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Muscle parvalbumin isoforms of Clarias gariepinus, Heterobranchus longifilis and Chrysichthys auratus : isolation, characterization and expression during development
Author(s) -
Focant B.,
Mélot F.,
Collin S.,
Chikou A.,
Vandewalle P.,
Huriaux F.
Publication year - 1999
Publication title -
journal of fish biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.672
H-Index - 115
eISSN - 1095-8649
pISSN - 0022-1112
DOI - 10.1111/j.1095-8649.1999.tb02036.x
Subject(s) - biology , clarias gariepinus , catfish , gene isoform , isoelectric point , larva , parvalbumin , microbiology and biotechnology , zoology , medicine , biochemistry , fishery , ecology , enzyme , fish <actinopterygii> , gene , genetics
The white‐muscle parvalbumin isoforms of Clarias gariepinus, Heterobranchus longifilis and Chrysichthys auratus were purified and their physicochemical parameters determined. The three catfish isoforms are distinct but those of C. gariepinus and H. longifilis are more similar. In the course of development, the successive appearance of larval and adult parvalbumins was observed. Larval isoforms (PA I, PA IIa, PA IIb) displayed a lower isoelectric point (pI) and molecular mass than adult ones (PA IIc, PA IIIa, PA IIIb, PA III, PA IV). The PA IIa isoform appeared as an omnipresent typical larval isoform. PA IIb appeared mostly larval, being insignificant in adult specimens; its physicochemical features were the same in the three catfish species. In Chrysichthys auratus , there were three PA II isoforms, one appearing as an adult isoform (PA IIc). The fact that the two types of parvalbumin isoforms appear at different times should reflect specific physiological needs (mobility, feeding) of different developmental stages.