Indian Journal of Biochemistry 
& Biophysics

 

Total visitors: 3,625  since 24-02-06

ISSN : 0301-1208

CODEN : IJBBBQ

VOLUME 43

NUMBER 1

FEBRUARY 2006

 

 CONTENTS

 

Papers

 

Antibodies against 9-O-acetylated sialic acids in childhood acute lymphoblastic leukemia: A two-year study with 186 samples following protocol MCP 943

7

      Suman Bandyopadhyay, Mitali Chatterjee, Shripad D Banavali, Santanu Pal, Chandrika N Nair, Suresh H Advani and Chitra Mandal*

 

 

 

Identification and characterization of a new putative c-type lysozyme from malaria vector Anopheles stephensi

15

      Rajnikant Dixit*, Sarita Dixit and Surendra Gakhar

 

 

 

Effect of vitamin E on monosodium glutamate induced hepatotoxicity and oxidative stress in rats

20

      Oscar Okwudiri Onyema*, Ebenezer Olatunde Farombi, Godwin O Emerole, Agwu Igwe Ukoha and Godffrey Okeke Onyeze

 

 

 

Antioxidant potential of C-phycocyanin isolated from cyanobacterial species Lyngbya, Phormidium and Spirulina spp.

25

      Anamika Patel, Sandhya Mishra* and P K Ghosh

 

 

 

Development of pharmacophoric model of condensed pyridine and pyrimidine analogs

      as hydroxymethyl glutaryl coenzyme A reductase inhibitors

32

      M Saxena, Love K Soni, Arun K Gupta, S R Wakode, A K Saxena and    S G Kaskhedikar*

 

 

 

Kinetics and mechanism of reduction of ferricytochrome c by glutathione

      and l-cysteine: A comparative study

37

      U Subudhi, G B N Chainy and P Mohanty*

 

 

 

Oxyradical accumulation and rapid deterioration of soybean seeds due to

      field weathering

41

      Sanjeev Yadav*, V S Bhatia and K N Guruprasad

 

 

 

Notes

 

Enzymatic characteristics of ligninperoxidases from Penicillium citrinum,

      Fusarium oxysporum and Aspergillus terreus using n-propanol as substrate

48

      Meera Yadav and K D S Yadav*

 

(Contd)

 

Kinetics and mechanisms of cholesterol esterase inhibition by cardiovascular drugs

      in vitro

52

      Shyh-Ying Chiou, Gin-Win Lai, Long-Yau Lin and Gialih Lin*

 

 

 

Book Review

56

 

 

Instructions to Authors

59

 

 

*Author for correspondence

 

AUTHOR INDEX

 

Advani S H

7

Banavali S D

7

Bandyopadhyay S

7

Bhatia V S

41

Chainy G B N

37

Chatterjee M

7

Chiou Shyh-Ying

52

Dixit S

15

Dixit R

15

Emerole G O

20

Farombi E O

20

Gakhar S

15

Ghosh P K

25

Gupta A K

32

Guruprasad K N

41

Kaskhedikar S G

32

Lai Gin-Win

52

Lin G

52

Lin Long-Yau

52

Mandal C

7

Mishra S

25

Mohanty P

37

Nair C N

7

Onyema O O

20

Onyeze G O

20

Pal S

7

Patel A

25

Saxena A K

32

Saxena M

32

Soni L K

32

Subudhi U

37

Ukoha A I

20

Wakode S R

32

Yadav S

41

Yadav K D S

48

Yadav M

48

 

 

 

 

          Papers

 

 

Indian Journal of Biochemistry & Biophysics

Vol. 43, February 2006, pp. 7-14

 

 

Antibodies against 9-O-acetylated sialic acids in childhood
acute lymphoblastic leukemia: A two-year study with 186 samples
following protocol MCP 943

Suman Bandyopadhyaya,#, Mitali Chatterjeeb, Shripad D Banavalic, Santanu Pala, Chandrika N Nairc, Suresh H Advanic and Chitra Mandala,*

Received 18 August 2005; ; revised 31 January 2006

Initial studies have revealed an enhanced surface expression of 9-O-acetylated sialoglycoconjugates (9-OAcSGs) on lymphoblasts concomitant with high titers of antibodies (anti-9-OAcSGs) in childhood acute lymphoblastic leukemia (ALL)1-4. This study was undertaken in 186 coded samples from 69 ALL patients to evaluate if antibodies against these sialoglycans could monitor response to the treatment. An ELISA was developed using bovine submaxillary mucin (BSM) containing high % of 9-O-acetylated sialic acids (9-OAcSA) as the capture antigen, to investigate serum levels of anti 9-OAcSGs in a single-center series of pediatric, clinically-diagnosed and immunophenotypically confirmed ALL patients, as compared to 130 healthy controls. At presentation, a 3.8-fold increase in anti-9-OAcSGs levels was detected in 63/69 ALL patients (mean ± SEM was 102.8 ± 6.3 mg/ml) as compared to normal controls (27.17 ± 0.76 mg/ml), assay sensitivity being 91.3%. On an individual basis (n = 25) in patients who were longitudinally monitored for two years, a significant decline in their mean ± SEM of OD405 was observed from 0.85 ± 0.06 to 0.28 ± 0.03. Additionally, a dot-blot was developed to evaluate the proportion of immune-complexed 9-OAcSGs in these patients employing achatinin-H, a 9-OAcSA-binding lectin. Our data indicate that these economically viable ELISA-based approaches allow for reliable, sensitive and rapid diagnosis of ALL. We contend that these disease-specific antibodies could be considered as potential markers both for the initial diagnosis of ALL and possibly for longitudinal monitoring of the disease.

Keywords: Acute lymphoblastic leukemia, 9-O-acetylated sialoglycoconjugates (9-OAcSGs), bovine submaxillary mucin,  achatinin-H, BSM-ELISA, Dot-blot

E-mail: cmandal@iicb.res.in or chitra_mandal@yahoo.com

 

Indian Journal of Biochemistry & Biophysics

Vol. 43, February 2006, pp. 15-19

 

 

Identification and characterization of a new putative c-type lysozyme
from malaria vector Anopheles stephensi

Rajnikant Dixit*, Sarita Dixit and Surendra Gakhar

Received 5 September 2005; revised 12 December 2005

Lysozyme (E.C. 3.2.1.17) activity is reported from the malaria vector Anopheles stephensi. The activity was detected in the salivary gland and midgut using bacteriolytic radial diffusion assay. Spectrophotometric analysis indicated that higher level of lysozyme activity was maintained in both midgut and salivary gland tissues. The activity reached the highest level in 4-8 days old mosquitoes. Genomic PCR amplification revealed the presence of at least two putative lysozyme genes in the mosquito genome. Preliminary analysis of one of the 413 bp genomic fragments showed 56% identity to the lysozyme of mosquito A. gambiae. However, the nature and origin of the putative cloned lysozyme gene remains elusive.

Keywords: Lysozyme, mosquito, malaria, salivary gland, midgut, Anopheles stephensi

IPC Code: C1N9/36

E mail: dixit2k@yahoo.com

 

Indian Journal of Biochemistry & Biophysics

Vol. 43, February 2006, pp. 20-24

 

Effect of vitamin E on monosodium glutamate induced hepatotoxicity and oxidative stress in rats

Oscar Okwudiri Onyema*, Ebenezer Olatunde Farombi#, Godwin O Emerole #,
Agwu Igwe Ukoha* and Godffrey Okeke Onyeze*

Received 14 June 2005; revised 7 December 2005

Monosodium glutamate (MSG), administered to rats (by gavage) at a dose of 0.6 mg/g body weight for 10 days, significantly {P<0.05) induced lipid peroxidation (LPO), decreased reduced glutathione (GSH) level and increased the activities of glutathione-s-transferase (GST), catalase and superoxide dismutase (SOD) in the liver of the animals; these were observed 24 hr after 10 days of administration. The activities of alanine aminotransferase (ALT), aspartate aminotransferase (AST) and γ glutamyl transferase (GGT) were also significantly increased in the serum, on MSG administration. Vitamin E (0.2 mg/g body wt) co-administered with MSG, significantly reduced the LPO, increased the GSH level and decreased the hepatic activities of GST, catalase and SOD. The activities of ALT, AST and GGT in the serum were also significantly reduced. The results showed that MSG at a dose of 0.6 mg/g body wt induced the oxidative stress and hepatotoxicity in rats and vitamin E ameliorated MSG-induced oxidative stress and hepatotoxicity.

Keywords: Monosodium glutamate, vitamin E, antioxidants, hepatotoxicity, oxidative stress.

IPC Code: C07D 311/72

E-Mail: oscarow@yahoo.co.uk

 

 

Indian Journal of Biochemistry & Biophysics

Vol. 43, February 2006, pp. 25-31

 

 

Antioxidant potential of C-phycocyanin isolated from cyanobacterial species Lyngbya, Phormidium and Spirulina spp.

Anamika Patel, Sandhya Mishra* and P K Ghosh

Received 11 May 2005; revised 13 December 2005

The antioxidant activity of C-Phycocyanin (C-PC) isolated from three cyanobacterial species Lyngbya (marine), Phormidium (marine) and Spirulina (fresh water) was studied in vitro. The results demonstrate that C-PCs from Lyngbya, Phormidium and Spirulina spp. are able to scavenge peroxyl radicals (determined by crocin bleaching assay) with relative rate constant ratio of 3.13, 1.89 and 1.8, respectively. C-PCs also scavenge hydroxyl radicals (determined by deoxyribose degradation assay) with second order rate constant values of 7.87 ´ 1010, 9.58 ´ 1010 and 6.42 ´ 1010, respectively. Interestingly, Lyngbya C-PC is found to be an effective inhibitor of peroxyl radicals (IC50 6.63 mM), as compared to Spirulina (IC50 12.15 mM) and Phormidium C-PC (IC50 12.74 mM) and is close to uric acid (IC50 2.15 mM). Further, the studies suggest that the covalently-linked tetrapyrrole chromophore phycocyanobilin is involved in the radical scavenging activity of C-PC. The electron spin resonance (ESR) spectra of C-PCs indicate the presence of free radical active sites, which may play an important role in its radical scavenging property. This is the first report on the ESR activity of native
C-PCs without perturbations that can cause radical formation.

Keywords:C-Phycocyanin, cyanobacteria, antioxidant, hydroxyl and peroxyl radical scavenger, electron spin resonance (ESR) spectra, Lyngbya, Phormidium, Spirulina

IPC Code:  A61K35/74

E.mail: smishracsmcri@rediffmail.com

 

Indian Journal of Biochemistry & Biophysics

Vol. 43, February 2006, pp. 32-36

 

Development of pharmacophoric model of condensed pyridine and pyrimidine analogs as hydroxymethyl glutaryl coenzyme A reductase inhibitors

M Saxena1, Love K Soni1, Arun K Gupta1, S R Wakode2, A K Saxena3 and S G Kaskhedikar1*

Received 5 May 2005; revised 31 October 2005

Quantitative structure-activity relationship (QSAR) has been established on a series of thirty-eight compounds of four different sets of condensed pyridine and pyrimidine analogs, for their hydroxymethyl glutaryl coenzyme (HMG-CoA) reductase inhibitor activity, in order to understand the essential structural requirement for binding with receptor, in terms of common biophoric and secondary sites employing APEX-3D software. Among several 3D pharmacophoric models with different sizes and arrangements, one model was selected based on r2 = 0.8, chance<0.001, match equivalent to 0.38 and all the 38 compounds were considered. The results suggest that hydrophobicity, hydrogen acceptor and optimum steric refractivity play a dominant role in the inhibition of HMG-CoA reductase. The information obtained from the present study can be used to design and predict more potent molecules as HMG-CoA reductase inhibitors, prior to their synthesis.

Keywords: Pharmacophore, 3D-QSAR, condensed pyridine and pyrimidine analogs, HMG-CoA reductase inhibitors, anti- hyperlipidemic agents

IPC Code: C12N9/99

E-mail: arunkg_73@hotmail.com

 

Indian Journal of Biochemistry & Biophysics

Vol. 43, February 2006, pp. 37-40

 

 

Kinetics and mechanism of reduction of ferricytochrome c by glutathione and l-cysteine: A comparative study

U Subudhi, G B N Chainy and P Mohanty*

Received 5 July 2005; revised 19 December 2005

The kinetics and mechanism of the reduction of ferricytochrome c [Cyt c(III)] by substrates namely glutathione (GSH) and l-cysteine (l-cys) have been investigated spectrophotometrically employing [substrate]T >> [Cyt c(III)]T. The reaction exhibits first order dependence in [substrate]T and  [Cyt c(III)]T. The pseudo-first order rate constant increases with an increase in pH, indicating that the conjugate base form of the HCyt c(III) is a better oxidant than the parent HCyt c(III). The electron transfer rate constants between the oxidants and GSH for both the k1 and k2 paths are found to be greater than that with l-cysteine. Hence, GSH is a better reductant of Cyt c(III) as compared to l-cysteine. A suitable mechanism has been proposed on the basis of experimental findings. The deprotonation constant for HCyt c(III) and the second order rate constants of k1 and k2 paths for the present reaction at 250C have been determined.

Keywords: Ferricytochrome c, glutathione, l-cysteine, reduction

IPC Code: C07K14/80

E-mail: prakashmohanty@rediffmail.com

 

Indian Journal of Biochemistry & Biophysics

Vol. 43, February 2006, pp. 41-47

 

Oxyradical accumulation and rapid deterioration of soybean seeds due to field weathering

Sanjeev Yadav1*, V S Bhatia2 and K N Guruprasad1

Received 13 June 2005; revised 23 January 2006

The effect of field weathering on oxyradical accumulation and subsequent changes were studied in the seeds of soybean [Glycine max (L.) Merr.] cv. JS 71-05. Electron spin resonance (ESR) quantification of oxyradical revealed that field weathering plays an important role in acceleration of their accumulation. One week of weathering increased the accumulation of oxyradicals to almost 2-fold and triggered the deteriorative cascade, by enhancing the lipid peroxidation and membrane perturbation, leading to cell death in seed tissues and poor germinability and vigour of soybean seeds. Thus, the weather conditions at the time of physiological maturity to harvesting of crop are very crucial and the field weathering plays a critical role for the maintenance of seed quality.

Keywords: Electron spin resonance (ESR) spectra, field weathering, membrane perturbation, lipid peroxidation, oxyradicals, spin trap, soybean, seed vigour

IPC Code: A23J 3/16

E-mail: sanjeev_kushu@yahoo.com

 

 

Indian Journal of Biochemistry & Biophysics

Vol. 43, February 2006, pp. 48-51

 

Notes

Enzymatic characteristics of ligninperoxidases from Penicillium citrinum, Fusarium oxysporum and Aspergillus terreus using n-propanol as substrate

Meera Yadav and K D S Yadav*

Received 23 September 2005; revised 10 December 2005

The activities of ligninperoxidases from Penicillium citrinum MTCC 3565, Fusarium oxysporum MTCC 3379 and Aspergillus terreus MTCC 3374 have been assayed and the enzymatic characteristics like Km, pH and temperature optima using n-propanol as the substrate have been reported. The results suggest that n-propanol can substitute veratryl alcohol as substrate for assaying ligninperoxidase activities from different fungal strains, without affecting the enzymatic characteristics. The above strains were selected, as they were known to secrete ligninperoxidase in the liquid culture medium.

Keywords: Ligninperoxidases, enzymatic characteristics, n-propanol, veratryl alcohol, Penicillium citrinum, Fusarium oxysporum, Aspergillus terreus

IPC Code:  C12N 9/28

E mail: kds_chemistry@rediffmail.com

 

Indian Journal of Biochemistry & Biophysics

Vol. 43, February 2006, pp. 52-55

 

Kinetics and mechanisms of cholesterol esterase inhibition by cardiovascular drugs in vitro

Shyh-Ying Chiou,a Gin-Win Lai,b Long-Yau Lina and Gialih Linb,*

Received 1 August 2005; revised 7 December 2005

Cardiovascular drugs such as lovastatin, simvastatin, amlodipine besylate, nifedipine, and hydralazine hydrochloride inhibit cholesterol esterase (CEase) in vitro. In the present paper, an attempt was made to determine kinetically the reaction mechanism for CEase inhibition by these drugs. The inhibition constant, Ki, for the mixed-type inhibition of CEase by these drugs in the presence of triton-X-100 or taurochloate were measured. Moreover, the pKi values were correlated with the molecular weights of these drugs. In conclusion, the fact that these drugs lower cholesterol levels in the plasma low-density lipoprotein may be partially due to the CEase inhibition by these drugs.

 

Keywords:                    Cholesterol esterase inhibition; enzyme kinetics; cardiovascular drugs.

IPC Code:                    C12N9/99

-mail: gilin@dragon.nchu.edu.tw

 

 

Indian Journal of Biochemistry & Biophysics

Vol. 43, February 2006, pp. 56-58

 

BOOK REVIEW

 

 

Advances in Photosynthesis and Respiration (AIPH), (Series Editor: Govindjee, University of Illinois, USA). Volume 22: “Photosystem II. The Light-Driven Water: Plastoquinone Oxidoreductase,” 2005 (Editors: Thomas J Wydrzynski, Australian National University, Australia and Kimiyuki Satoh, Okayama University, Japan; and Tech. Asst. Editor: Joel A Freeman, Springer); Published by Springer, The Netherlands, ISBN 1–4020–4249-3; Hardbound pp 775 (plus 8 page Index), Price, Euro 295 (approx. INR 18,000/-). A 25% discount is given for International Society of Photosynthesis Research (ISPR) members.