Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/3709
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)
Lipoprotein
⍺-foetoprotein
Sulfhydryls
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.
Description: 148-153
URI: http://hdl.handle.net/123456789/3709
ISSN: 0301-1208
Appears in Collections:IJBB Vol.41(4) [August 2004]

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