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Biochim Biophys Acta 1975 Mar 28;3861:260-9. doi: 10.1016/0005-2795(75)90267-6.
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Purification of a carboxypeptidase B-like enzyme from the starfish Dermasterias imbricata.

Ferrell RE , Camacho Z , Kitto GB .

A carboxypeptidase B-like enzyme which catalyses the hydrolysis of synthetic esters of lysine and arginine has been isolated from the starfish Dermasterias imbricata. This carboxypeptidase B-like enzyme has a molecular weight of approximately 34 000 and shares this and other properties with bovine pancreatic carboxypeptidase B. The existence of zymogen for this activity in the pyloric caeca of the starfish is demonstrated. This zymogen has a molecular weight near 40 000 and appears to be analogous to other monomeric procarboxypeptidases B. The zymogen possesses an intrinsic low-level activity toward synthetic substrates of carboxypeptidase B and is activated by trypsin.

PubMed ID: 236021
Article link: Biochim Biophys Acta

Genes referenced: LOC574780 LOC579470