Website address: wwwniscairresin

 

Indian Journal of Biochemistry & Biophysics

CODEN : IJBBBQ  ISSN : 0301-1208

 

VOLUME 45

NUMBER5

OCTOBER 2008

 
    CONTENTS

 

 

Minireview

 

Melatonin: Fifty Years of Scientific Journey from the Discovery in Bovine Pineal Gland to Delineation of Functions in Human

289

Indrajit Chowdhury, Anamika Sengupta and Saumen Kumar Maitra*

 

 

 

Papers

 

Molecular cloning, expression and characterization of a-amylase gene from  a marine bacterium Pseudoalteromonas sp. MY-1

305

         Xueying Tao, Moon-Sun Jang, Kyoung-Sook Kim, Ziniu Yu and
Young-Choon Lee*

 

 

 

Plastocyanin microheterogeneity in Scenedesmus acutus MT8

310

Mitko I Dimitrov*, Anthony A Donchev, Georgi R Toromanov, Vladimir I Getov and Tonka G Toncheva-Panova

 

 

 

Curcumin-induced recovery from hepatic injury involves induction of apoptosis of activated hepatic stellate cells

317

         S Priya and P R Sudhakaran*

 

 

 

Effects of various extremely low frequency magnetic fields on the free radical processes, natural antioxidant system and respiratory burst system activities in the heart and liver tissues

326

Ayse Gulnihal Canseven*, Sule Coskun and Nesrin Seyhan

 

 

 

Protective effect of taurine and quercetin against renal dysfunction associated with the combined use of gentamycin and diclofenac

332

Adel A Kheir Eldin, Amira A. Shaheen, Hanan M Abd Elgawad* and
Nagwa I Shehata

 

 

 

Notes

 

Suppressive effect of Strychnos nux-vomica on induction of ovalbumin-specific IgE antibody response in mice

341

         Govinda Rao Duddukuri*, A Naga Brahmam and D N Rao

 

 

 

Enzymatic characteristics of quercetinases from some indigenous Aspergillus flavus strains

345

         R S S Yadav and K D S Yadav*

 

 

 

Kinetics of α-chymotrypsin catalyzed hydrolysis of 4-nitrophenyl acetate
in ethanolamine surfactants

350

         Kallol K Ghosh* and Santosh Kumar Verma

 

 

 

Book review

354

 

 

Instructions to Authors

356

 

 

——————

*Author for correspondence

 

 

                         AUTHOR INDEX

 


Brahmam A N

341

Canseven A G

326

Chowdhury I

289

Coskun S

326

Dimitrov M I

310

Donchev A A

310

Duddukuri G R

341

Eldin A A K

332

Elgawad H M A

332

Getov V I

310

Ghosh K K

350

Jang M-S

305

Kim K-S

305

Lee Y-C

305

Maitra S K

289

Priya S

317

Rao D N

341

Sengupta A

289

Seyhan N

326

Shaheen A A

332

Shehata N I

332

Sudhakaran P R

317

Tao X

305

Toncheva-Panova T G

310

Toromanov G R

310

Verma S K

350

Yadav K D S

345

Yadav R S S

345

Yu Z

305


 

 

 

 

MINIREVIEW

 

 

Indian Journal of Biochemistry & Biophysics

Vol. 45, October 2008, pp. 289-304

 

 

Melatonin: Fifty Years of Scientific Journey from the Discovery in Bovine Pineal Gland to Delineation of Functions in Human

Indrajit Chowdhury1, Anamika Sengupta2 and Saumen Kumar Maitra3*

1Department of Obstetrics and Gynecology, 2Department of Physiology, Morehouse School of Medicine, Atlanta, USA

3Department of Zoology, Visva-Bharati University, Santiniketan, 731 235, India

 

Received 24 November 2007; revised 01 July 2008

Melatonin (N-acetyl-5-methoxytryptamine) was first purified and characterized from the bovine pineal gland extract by Aron Lerner and co-workers in 1958. Since then, a plethora of information has piled up on its biosynthesis, metabolism, time-bound periodicity, physiological and patho-physiological functions, as well as its interactions with other endocrine or neuro-endocrine organs and tissues in the body. Melatonin has wide range of applications in physiology and biomedical fields. In recent years, a significant progress has been made in the understanding mechanism of its actions at the cellular and molecular levels. Consistent efforts have uncovered the mystery of this indoleamine, and demonstrated its role in regulation of a large as well as diverse body functions in different groups of animals in general, and in humans in particular. Current review, in commemoration of 50 years of discovery of melatonin, while revisiting the established dogmas, summarizes current information on biosynthesis, secretion, metabolism and molecular mechanism of action of melatonin at cellular level and highlights the recent research on its role in human physiology and clinical biology.

          Keywords: AA-NAT, Biological rhythm, Cancer, Melatonin, Pineal gland, Reproduction, Seasonal affective  disorder Suprachiasmatic nucleus, Sleep, Jet-lag

*E-mail: dgp_skmaitra@yahoo.co.in, skmaitra@visva-bharati.ac.in

 

 

PAPERS

 

 

Indian Journal of Biochemistry & Biophysics

Vol. 45, October 2008, pp. 305-309

 

 

Molecular cloning, expression and characterization of a-amylase gene from a marine bacterium Pseudoalteromonas sp. MY-1

Xueying Tao1,2, Moon-Sun Jang1, Kyoung-Sook Kim1, Ziniu Yu2 and Young-Choon Lee1*

1Department of Biotechnology, College of Natural Resources and Life Science, Dong-A University, Busan 604-714, South Korea

2State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China

Received 25 April 2008; revised 23 August 2008

A gene (amyA) encoding an extracellular a-amylase from a marine bacterium Pseudoalteromonas sp. MY-1 was cloned and expressed in Escherichia coli. It comprised an open-reading-frame of 2,007 base pairs and encoded a protein of 669 amino acids with a predicted molecular weight of 73,770 daltons and a pI of 5.15. The entire amino acid sequence of amyA gene showed 86% similarity to the a-amylase preproprotein from Pseudoalteromonas haloplanktis. It consisted of a signal peptide, α-amylase catalytic domain and an amy C domain. The recombinant amylase was purified to homogeneity and biochemically characterized. The enzyme revealed maximum activity at pH 7.0 and 40şC. The enzyme hydrolyzed soluble starch and some maltooligosaccharides to several oligosaccharides, and maltose was the common product from different substrates.

Keywords: Pseudoalteromonas, a Amylase, Cloning, Characterization

*E-mail: yclee@dau.ac.kr

 

 

Indian Journal of Biochemistry & Biophysics

Vol. 45, October 2008, pp. 310-316

 

 

Plastocyanin microheterogeneity in Scenedesmus acutus MT8

Mitko I Dimitrov1*, Anthony A Donchev1, Georgi R Toromanov1, Vladimir I Getov1
and Tonka G Toncheva-Panova2

1Institute of Biophysics, Bulgarian Academy of Sciences, Sofia-1113, Bulgaria

2Institute of Plant Physiology, Bulgarian Academy of Sciences, Sofia-1113, Bulgaria

 

Received 30 October 2007; revised 29 August 2008

Two total plastocyanin (PC) fractions — loosely bound (lPC) and strongly bound (sPC) were extracted (84% and 16%, respectively) from the homogenate of Scenedesmus acutus MT8. Two-fold isolation-purification procedure including DE-52 chromatography separated lPC into a smaller oxidized [lPC (II)] and a larger reduced [lPC(I)] fractions, in contrast to sPC, where sPC(II) greatly dominated over sPC(I). Analytical isoelectric focusing (IEF) separated lPC(II) into two main fractions only in the presence of 8 M urea, implying microheterogeneity. Preparative IEF in immobiline pH-gradient of 3.2-4.1 separated lPC(II) into two blue fractions – a more alkaline lPC'(II) and a more acidic lPC''(II), which were probably stereoisomers. Their UV-Vis spectra exhibited rarely observed tryptophane (291.5 nm) and some differences at 270 and 287 nm. The exact molecular masses of apo-/holo-lPC (10131 Da/10194 Da) were determined by mass spectrometry. The number of -SH groups was determined from the mass difference between alkylated with 4-vinylpyridine (4-VP) and non-alkylated protein. Additionally, a simple procedure for simultaneous separation of both primary structure and stereoisomers of PC was developed.

 

Keywords: Plastocyanin, Microheterogeneity, Dimorphism, Isoelectric focusing, Chromatofocusing

*E-mail: mitkod@bio21.bas.bg

 

 

Indian Journal of Biochemistry & Biophysics

Vol. 45, October 2008, pp. 317-325

 

 

Curcumin-induced recovery from hepatic injury involves induction of apoptosis of activated hepatic stellate cells

S Priya and P R Sudhakaran*

Department of Biochemistry, University of Kerala, Kariavattom, Thiruvananthapuram, India, 695 581

 

Received 14 May 2007; revised 28 July 2008

Hepatic stellate cells (HSCs) undergo activation and transdifferentiation to myofibroblast like cells in liver injury, leading to liver fibrosis. During recovery from injury, activated HSCs may either revert back to quiescent state or undergo apoptosis or both. In the present study, we have examined whether recovery from hepatic injury involves apoptosis of activated HSCs and tested whether curcumin (the yellow pigment from Curcuma longa Linn.) promotes recovery from hepatic injury by inducing apoptosis of these cells. Hepatic injury was induced by CCl4 and apoptosis was studied in HSCs isolated from liver by MTT assay, DNA fragmentation, and DAPI and annexin staining. Hepatic recovery was assessed by measuring hepatic marker activities, such as serum GOT, GPT and protein. Hepatic recovery occurred within 4 weeks after inducing injury in untreated control, whereas curcumin treatment caused hepatic recovery within 2 weeks, as evidenced by the reduction of hepatic marker activities to near normal levels. HSCs isolated from liver of animals treated with curcumin showed maximum apoptotic marker activities in 2nd week, whereas in HSCs from untreated control recovering from injury, maximum apoptosis was observed in 4th week. Induction of apoptosis in vivo during hepatic recovery was also suggested by increase in caspase-3 activity. Treatment of isolated HSCs in culture with curcumin caused apoptosis during later stages confirming that curcumin induced apoptosis of activated HSCs and not in unactivated quiescent HSCs. These results suggested that hepatoprotective effect of curcumin causing recovery from injury involved apoptosis of activated HSCs.

Keywords: Hepatic stellate cells, Apoptosis, Curcumin, Hepatic fibrosis, Retinol

*E-mail: prsbn@md4.vsnl.net.in

 

 

Indian Journal of Biochemistry & Biophysics

Vol. 45, October 2008, pp. 326-331

 

 

Effects of various extremely low frequency magnetic fields on the free radical processes, natural antioxidant system and respiratory burst system activities in the heart and liver tissues#

Ayse Gulnihal Canseven1*, Sule Coskun2 and Nesrin Seyhan1

1Department of Biophysics, Gazi University, Faculty of Medicine & GNRP Center, Ankara, Turkey

2Department of Biology, Gazi University, Faculty of Art and Science, Ankara, Turkey

 

Received 04 January 2008; revised 19 July 2008

Magnetic fields (MFs) can affect biological systems by increasing the release of free radicals that are able to alter cell defense systems and breakdown tissue homeostasis. In the present study, the effects of extremely low frequency (ELF) electromagnetic fields (EMF) were investigated on free radical levels, natural antioxidant systems and respiratory burst system activities in heart and liver tissues of guinea pigs exposed to 50 Hz MFs of 1, 2 and 3 mT for 4 h/day and 8 h/day for 5 days by measuring malondialdehyde (MDA), nitric oxide (NO), glutathione (GSH) levels and myeloperoxidase (MPO) activity. A total of sixty-two male guinea pigs, 10-12 weeks old were studied in seven groups as control and exposure groups: Group I (control), II (1 mT, 4 h/day), III (1 mT, 8 h/day), IV (2 mT, 4 h/day), V (2 mT, 8 h/day), VI (3 mT, 4 h/day), and VII (3 mT, 8 h/day). Controls were kept under the same conditions without any exposure to MF. MDA levels increased in liver in groups II and IV, but decreased in group VII for both liver and heart tissues. NOx levels declined in heart in groups II and III and in liver in groups III, V, and VI, but increased in liver in group VII. GSH levels increased in heart in groups II, IV, V, and in liver in groups V and VI and VI, but decreased in groups II and IV in liver. MPO activity decreased in liver in groups III, IV, VI and VII with respect to controls and in heart tissues in groups II, III and IV; however, there was a significant increase MPO activity in heart in group VII. From the results, it can be concluded that the intensity and exposure duration of MFs are among the effective conditions on the formation of free radicals and behaviour of antioxidant enzymes.

Keywords: Extremely low frequency, Electromagnetic fields, Free radicals, MDA, NOx, GSH, Myeloperoxidase activity

*E-mail: canseven@gazi.edu.tr, agcanseven@gmail.com; aysecanseven@hotmail.com

 

 

Indian Journal of Biochemistry & Biophysics

Vol. 45, October 2008, pp. 332-340

 

 

Protective effect of taurine and quercetin against renal dysfunction associated
with the combined use of gentamycin and diclofenac

Adel A Kheir Eldin, Amira A. Shaheen, Hanan M Abd Elgawad* and Nagwa I Shehata

Department of Biochemistry, Faculty of Pharmacy, Cairo University, Cairo, Egypt

 

Received 12 March 2008; revised 26 August 2008

The potential protective effects of taurine and quercetin against gentamycin (GM)/diclofenac (DC) combined nephrotoxicity were investigated in rats. The results showed that administration of DC alone at an oral dose of 5 mg/kg b.wt/day for 28 days had no significant effect on the measured parameters, except for marked increase in urinary uronic acid excretion. Administration of GM alone at a dose of 100 mg/kg b.wt/day i.p. for 8 days resulted in obvious nephrotoxicity. Combined GM-DC treatment led to the most pronounced nephrotoxicity, as indicated by greater elevations in serum urea, creatinine and urinary N-acetyl-β-D-glucosaminidase (NAG), together with severe depression of renal cortical Na+, K+-ATPase, compared to GM-treated group. Moreover, only combined treatment resulted in significant decrease in urinary potassium and renal cortical glutathione peroxidase (GSHPx), together with an increase in renal cortical lipid peroxidation products (LPOs). Co-administration of taurine or quercetin normalized creatinine clearance and ameliorated the elevations in urinary proteins, uronic acids, NAG and renal cortical LPOs in GM/DC treated rats. The study justifies the use of taurine and quercetin as renoprotective agents against the nephrotoxicity caused by GM/DC therapy.

 

Keywords: Nephrotoxicity, Gentamycin, NSAIDs, Taurine, Quercetin

*E-mail: hananabdelgawad@yahoo.com

 

 

NOTES

 

 

Indian Journal of Biochemistry & Biophysics

Vol. 45, October 2008, pp. 341-344

 

 

Suppressive effect of Strychnos nux-vomica on induction of ovalbumin-specific IgE antibody response in mice#

Govinda Rao Duddukuri*, A Naga Brahmam and D N Rao+

Department of Biochemistry, GITAM University, Visakhapatnam 530 045, Andhra Pradesh, India

+Department of Biochemistry, AIIMS, New Delhi 110 029

 

Received 29 October 2007; revised 10 September 2008

Strychnos nux-vomica Linn. (SNV; Loganiaceae), a medicinal plant has been used as folk medicine for alleviating inflammation, joint pains and allergic symptoms. In the present study, we examined its possible immunomodulatory effect on induction of ovalbumin (OVA)-specific IgE antibody response in a murine model, as evaluated by passive cutaneous anaphylaxis (PCA). The OVA-specific IgE antibody response was significantly suppressed in BALB/c mice (H-2d), following intraperitoneal administration of aqueous stem extract of the plant along with OVA. Furthermore, the different doses of SNV extract were found to significantly suppress the induction of OVA-specific IgE antibody response. The anti-OVA IgE antibody response was suppressed in different haplotypes of mice viz., C57BL/6 (H-2b) and SWR/J(H-2q). However, preliminary findings revealed no significant change in the total IgG antibody response against OVA, as evaluated by ELISA. These results confirm the suppressive activity of S. nux-vomica on allergen-specific IgE antibody response and suggest its possible application in allergic conditions.

Keywords: Strychnos nux-vomica, Immunomodulation, Immunosuppression, IgE antibody response, Passive cutaneous anaphylaxis, ELISA

*E-mail: dgrao@rediffmail.com

 

 

Indian Journal of Biochemistry & Biophysics

Vol. 45, October 2008, pp.345-349

 

 

Enzymatic characteristics of quercetinases from some indigenous
Aspergillus flavus strains

R S S Yadav and K D S Yadav*

Department of Chemistry, D D U Gorakhpur University, Gorakhpur 273 009, India

 

Received 16 April 2007; revised 18 August 2008

 

Five indigenous Aspergillus flavus strains MTCC-2206, 1884, 1883, 1783 and 2456 were screened for the secretion of quercetinase. Fungal strains MTCC-2206, 1884, 1883, and 1783 were found to secrete the quercetinase in the range of 0.24-0.36 enzyme unit/mL of the culture medium, while MTCC-2456 secreted only 0.04 enzyme unit/mL. The enzymatic characteristics of quercetinase were determined. The Km values using quercetin as the substrate were 12.5 µM, 14.0 µM, 12.5 µM and 13.0 µM for the quercetinase produced by MTCC-2206, 1884, 1883 and 1783, respectively. The pH optima for the above enzymes were 6.5, 6.5, 6.0 and 6.0 and temperature optima were 45, 40, 45 and 50şC, respectively. The partial purification from only one strain MTCC-2206 was achieved (nearly 3-fold purification).

Keywords: Quercetinase, Aspergillus flavus, Dioxygenase, Copper enzyme

*E-mail: kds_chemistry@rediffmail.com

 

 

Indian Journal of Biochemistry & Biophysics

Vol. 45, August 2008, pp.350-353

 

 

Kinetics of α-chymotrypsin catalyzed hydrolysis of 4-nitrophenyl acetate in ethanolamine surfactants#

Kallol K Ghosh* and Santosh Kumar Verma

School of Studies in Chemistry, Pt. Ravishankar Shukla University, Raipur (C.G.), 492010, India

 

Received 19 November 2007; revised 13 August 2008

The kinetics of α-chymotrypsin (α-CT) catalyzed hydrolysis of 4-nitrophenyl acetate has been studied in aqueous solution of alkyldimethylethanolammonium bromide (cetyl, dodecyl, decyl) surfactants at concentrations below and above their critical micelle concentration. From Michaelis-Menten kinetics, the catalytic rate constant kcat and the Michaelis constant KM have been determined. The bell-shaped profiles of α-CT activity with increasing surfactant concentrations indicate the interaction between the micelle-bound enzyme and substrate.

Keywords: α-Chymotrypsin, 4-Nitrophenyl acetate, Hydrolysis, Micellar enzymology, Alkyldimethyl ethanol-ammonium bromide, Surfactants

E-mail: sqin@ms.qdio.ac.cn

 

 

Indian Journal of Biochemistry & Biophysics

Vol. 45, August 2008, pp.354-355

 

 

Book Review

 


Advances in Photosynthesis and Respiration (AIPH) (Series Editor: Govindjee, University of Illinois, USA). Volume 26: “Biophysical Techniques in Photosynthesis II (Edited by Thijs J Aarsma and Jörg Matysik);  Published by Springer, The Netherlands, 2008. ISBN: 976-1-4020-8249-8 (hardcover), 520 pages, & colour plates.
Price: 219 Euro.

The AIPH (Advances in Photosynthesis and Respiration) series, Vol. 26 titled, “Biophysical Techniques in Photosynthesis II” edited by
T J Aartsma & J Maysik, University of Leiden brings about new developments in the biophysical tools and techniques, and how they could reveal the finer and deeper details of the mechanism of photosynthesis. It contains 24 attractive and authoritative chapters contributed by 54 experts from 10 counties. The chapters have been clubbed under 5 thematic heads.

The first section (4 chapters) of the book covers tools and techniques on imaging — which is very familiar now in the medical field. Atomic force microscopy (AFM), 3D electron microscopy (EM), electron tomography and femtosecond laser coupled optical microscopy (applications of non-linear contrast mechanism to optical microscopy) are included in this section and these would tempt biologists of all descriptions in using them. A chapter on MRI of plants for reporting water transport and water balance in relation to photosynthesis adds value.

The second section (5 chapters) dwells on techniques for elucidating structures, especially those on stabilizing membrane proteins like plant light-harvesting complexes, and X-ray crystallography of photosynthetic proteins. Discussions on electron crystallography details about analyzing crystals by EM-based methods as an alternate to X-ray crystallography and NMR spectroscopy have been provided. The chapter on X-ray scattering measurements explains the need for knowing amplitudes and time scale of molecular motions, supplementing the detailed structural elucidation by X-ray crystallography.

The 3rd part of the book (4 chapters) deals with optical spectroscopy such as time-resolved infrared spectroscopy, non-linear femtosecond optical spectroscopy techniques, subpicoseond fluorescence spectral evolution using a streak camera and target analysis and optical spectroscopy of an individual photosynthetic light-harvesting complexes. These techniques and protocols enable unraveling of the pathways and dynamics of energy transfer processes. It appears that these experimental tools and protocols would encourage more rigorous experimentation on linking ultra-fast energy transfer, and electron and proton transfer dynamics. Further, the single molecule detection technique has been successfully used for individual light-harvesting complex of purple photosynthetic bacteria. The beauty of electronic structure of molecular aggregates in “producing efficient energy conversion” systems is shown in this section.

The penultimate 4th section (6 chapters) is devoted to the applications of magnetic resonance spectroscopy. The high field and high frequency electron paramagnetic resonance (EPR), involving single and multiple transitions are attractive additions for EPR users. The breakthroughs in pulsed microwaves, swappable cryomagnets, and fast data acquisition systems have been highlighted in these chapters. Illustrative examples on how these techniques are complementary to protein crystallography, solid-state NMR as well as optical spectroscopic methods, distance measurements in the photosynthetic reaction centers in bacteria, and the use of site-directed spin labeling techniques for probing structural and conformational patterns in photosynthetic machinery are new and fascinating.

The last section (5 chapters) is on theoretical treatments of spectroscopic methods and their recent advancements. Advancements, particularly on calculations of electrostatic energy, energy transfer and molecular dynamics, and on some newly developed quantum chemical methods have been covered. This section would be of considerable value to researchers interested in theory and modeling.

The present volume of AIPH series is a timely addition as a vital reference book for courses and programmes on physics, physical chemistry, biochemistry, biotechnology, biophysics, agricultural engineering and microbiology, life sciences, environmental sciences and ecology. It must be stated that the plant biophysics is an emerging strong discipline in plant sciences. Such type of techniques-based books are very useful for such advance undergraduate and graduate programmes. All the contributors have done excellent job. They have been successful in giving rigor to theoretical treatments as well as giving an overall perception of how these techniques reveal new dimension to a biologic process such as photosynthesis. Each chapter invites the readers to visualize a new direction in the specified field, and the two editors have done best to bridge different topics into coherent themes and sections. This reviewer strongly recommends that departments, colleges, universities and institutes (traditional and professionals) should have copies of this valuable book on biophysical techniques. Springer does bring excellence in publishing high quality books and journals, and this one adds their consistency. However, for students at large the cost is prohibitory.

 

Prasanna Mohanty

INSA Honorary Scientist at RPRC, Bhubaneswar, India 751015 and

Courtesy-Professor, Functional Biology, DAVV Indore, India 452 001

Formerly at JNU New Delhi, India

photosis@rediffmail.com


 

 



Indian Journal of Biochemistry & Biophysics

Editorial Board

Prof J Gowrishankar
Centre for DNA Fingerprinting and Diagnosis
Hyderabad 500 076

Prof M N Gupta
Department of Chemistry
Indian Institute of Technology
New Delhi 110 016

Prof Seyed E Hasnain
University of Hyderabad
 Hyderabad 500 046

Prof R V Hosur
Department of Chemical Sciences
Tata Institute of Fundamental Research
Homi Bhaba Road

Mumbai 400 005

Prof Young-Choon Lee
Department
of Biotechnology
Agricultural Resources and Life Science Research Institute

Dong-A University

Busan, Korea

 

Prof P C Mishra
Department of Physics
Banaras Hindu University
Varanasi 221 005

Prof K Muniyappa
Department of Biochemistry
Indian Institute of Science
Bangalore 560 012

Prof N S Punekar
Biotechnology Group, SBB
Indian Institute of Technology, Bombay
Mumbai 400 076

Prof D N Rao
Department of Biochemistry
All India Institute of Medical Sciences
New Delhi 110029

Prof M Saleemuddin
Department of Biochemistry
Faculty of Life Science
Aligarh Muslim University
Aligarh 202 002

Dr. Hari S Sharma

Erasmus M C
University Medical Center

Rotterdam
The Netherlands

 

Prof S Sivakami
Department of Life Sciences
University of Mumbai
Mumbai
400 098

Prof Avadhesha Surolia
National Institute of Immunology
New Delhi 110 067

Prof Umesh Varshney
Department of Microbiology & Cell Biology
Indian Institute of Science
Bangalore 560 012

Director, NISCAIR

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Published by the National Institute of Science Communication and Information Resources (CSIR), Dr K S Krishnan Marg, New Delhi 110 012

The Indian Journal of Biochemistry & Biophysics is issued bimonthly. The institute assumes no responsibility for the statements and opinions advanced by contributors. The editorial staff in its work of examining papers received for publication is assisted, in an honorary capacity, by a large number of distinguished scientists. Communications regarding contributions for publication in the journal should be addressed to the Editor, Indian Journal of Biochemistry & Biophysics, National Institute of Science Communication and Information Resources, Dr K S Krishnan Marg, New Delhi 110 012. All correspondence regarding reprints, journal copies, subscription renewals, claims for missing numbers and advertisements should be addressed to the Sales & Distribution Officer, National Institute of Science Communication and Information Resources, Dr K S Krishnan Marg, New Delhi 110 012. Payments may be made by money order, cheque, bank draft or postal order marked payable to National Institute of Science Communication and Information Resources,
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