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- W2078310708 abstract "Carboxypeptidase Y (E.C.3.4.12.1) with the lysine side-chains blocked by citraconylation has been digested with trypsin and the resulting peptides purified by gel filtration followed by ion-exchange chromatography on DE 52 cellulose. Eight of the expected ten peptides have been completely or partially sequenced in a liquid phase automatic sequencer. The remaining two peptides were sequenced as part of a CNBr peptide (see preceeding paper). Selected peptides obtained from enzymatic cleavages with A. mellea protease, chymotrypsin, post-proline cleaving enzyme, S. aureus V8 protease, and subtilisin have upon sequencing provided overlaps which have made the reconstruction of 96% of the complete sequence possible together with a tentative assignment of the carbohydrate attachment sites. No homology with sequences of known proteases has been observed." @default.
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- W2078310708 date "1982-01-01" @default.
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- W2078310708 title "Amino acid sequence of carboxypeptidase Y. II. Peptides from enzymatic cleavages" @default.
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- W2078310708 doi "https://doi.org/10.1007/bf02907794" @default.
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