| Literature DB >> 1080707 |
J P Capony, J Demaille, C Pina, J F Pechère.
Abstract
The primary structure of the most acidic (pI - 4.50) of the two major parvalbumins from frog (Rana esculenta) has been determined from a study of its trypsic peptides and of overlapping peptides generated by limited trypsic digestion, chymotrypsic digestion and N-bromosuccinimide cleavage of the protein. The amino acid sequence so obtained is considered in comparison with those known for other parvalbumins and for rabbit troponin-C.Entities:
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Year: 1975 PMID： 1080707 DOI： 10.1111/j.1432-1033.1975.tb02224.x
Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956