Abstract
Crystalline turkey trypsin has been characterized with respect to amino acid composition, end groups, and sequence of amino acids in the vicinity of its three histidine residues. Although amino acid composition and peptide maps indicated dissimilarities in primary structure from mammalian trypsins, the N- and C-terminal residues of turkey trypsin, isoleucine and asparagine, respectively, were identical to those of bovine and porcine trypsin. Five histidine-containing peptides were isolated from a peptic digest of the acid-insoluble core prodviced by the tryptic digestion of reduced and carboxymethylated turkey trypsin. From these five peptides the sequence of amino acids surrounding the three histidine residues could be reconstructed. A high degree of structural homology of these sequences with the histidine regions of bovine and porcine trypsin was evident.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
