NISCAIR Online Periodicals Repository

Research Journals >
Indian Journal of Biochemistry and Biophysics (IJBB) >
IJBB Vol.41 [2004] >
IJBB Vol.41(4) [August 2004] >

Title: Biochemical characterization of a protein of albumin multigene family from serum of African catfish Clarias gariepinus Bloch
Authors: Hasnain, Absar-ul
Ahmad, Riaz
Jabeen, Mumtaz
Khan, M Mushahid
Keywords: Biochemical characterization
Ligand transport
Catfish serum albumin (CfSA)
Human serum albumin (HSA)
Circular dichroism
Bilirubin binding
Helix topography
Clarias gariepinus
Issue Date: Aug-2004
Publisher: CSIR
Abstract: A monomorphic albumin-like protein (CfSA) has been purified to homogeneity from the serum of African air-breathing catfish Clarias gariepinus Bloch. It has a molecular mass of ≅70 kD and shows a lesser electrophoretic mobility than human serum albumin (HSA) in native gels. The protein exhibits cross-reactivity against rabbit anti-HSA serum and shows considerable similarity with HSA in secondary structure, however, with some differences, as indicated by a slight shift in the peaks around 267 nm and 278 nm and the absence of shoulders at 276 and 283. A certain degree of similarity also exists between their tertiary structures with respect to aromatic asymmetric environment as indicated by far-UV CD spectra and the visible range CD spectra of bilirubin complexes. CfSA-bilirubin complex is mainly characterized by bisignate CD Cotton effects (CDCEs), having minima and maxima wavelengths at 406 and 486 nm, respectively and unlike HSA, it shows prominent additional maxima around 426 nm. Based on the number of sulfhydryls, CfSA is in the rank of advanced teleosts. The occurrence of albumin in C. gariepinus in relation to the evolutionary dichotomy of albumin and other members of its multigene family in class Pisces has been discussed.
Page(s): 148-153
ISSN: 0301-1208
Source:IJBB Vol.41(4) [August 2004]

Files in This Item:

File Description SizeFormat
IJBB 41(4) 148-153.pdf246.94 kBAdobe PDFView/Open
 Current Page Visits: 90 
Recommend this item


Online Submission of Articles |  NISCAIR Website |  National Knowledge Resources Consortium |  Contact us |  Feedback

Disclaimer: NISCAIR assumes no responsibility for the statements and opinions advanced by contributors. The editorial staff in its work of examining papers received for publication is helped, in an honorary capacity, by many distinguished engineers and scientists.

CC License Except where otherwise noted, the Articles on this site are licensed under Creative Commons License: CC Attribution-Noncommercial-No Derivative Works 2.5 India

Copyright © 2015 The Council of Scientific and Industrial Research, New Delhi. All rights reserved.

Powered by DSpace Copyright © 2002-2007 MIT and Hewlett-Packard | Compliant to OAI-PMH V 2.0

Home Page Total Visits: 162271 since 01-Sep-2015  Last updated on 21-Jun-2016Webmaster: