| Literature DB >> 7295770 |
J Bonicel, P Couchoud, E Foglizzo, P Desnuelle, C Chapus.
Abstract
The complete sequence of the 96 residues composing horse colipase B has been determined by automated analysis of the intact protein, of two CNBr peptides and two tryptic peptides arising, respectively, from the citraconylated chain and from the unreduced protein. The single histidine of the protein is located at position 29 as in horse colipase A. His86, present in the C-terminal region of the pig cofactor and supposed to play a role in the folding molecule, is not conserved in horse B. Large pieces of the pig and horse B chains were found to be identical or very similar, especially the N-terminal sequence and the central segment Ala49-Cys65 including the three tyrosines of the molecule. The four lysines and the ten half cystines are also conserved.Entities:
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Year: 1981 PMID: 7295770 DOI: 10.1016/0005-2795(81)90221-x
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002