{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T03:06:14Z","timestamp":1767927974343,"version":"3.49.0"},"reference-count":33,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2005,3,3]],"date-time":"2005-03-03T00:00:00Z","timestamp":1109808000000},"content-version":"vor","delay-in-days":5905,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[1989,1]]},"abstract":"<jats:p>The human plasma metallo\u2010protease carboxypeptidase N of M<jats:sub>r<\/jats:sub> 280 000 consists of two small, enzymatically active subunits of M<jats:sub>r<\/jats:sub> 50 000 and two large subunits. Only the large subunits are glycosylated. They may have a function in stabilizing the complex in plasma. The N\u2010terminal sequence of the small subunit was determined from the isolated protein and used to specify a unique 59\u2010mer oligonucleotide probe. A cDNA clone of 1.7 kbp containing the entire coding sequence of the small subunit of carboxypeptidase N was isolated from a human\u2010liver cDNA library. The cDNA clone encodes a signal sequence of 20 amino acids and the 438 aminc acids of the mature subunit. There is a remarkable primary structure similarity of 49% to bovine carboxypeptidase E (enkephalin convertase). A more distant relationship to the bovine pancreatic, digestive carboxypeptidases A and B or even to the metallo\u2010endopeptidases is based mainly on the occurrence of conserved, mechanistically important residues.<\/jats:p>","DOI":"10.1111\/j.1432-1033.1989.tb14488.x","type":"journal-article","created":{"date-parts":[[2005,3,4]],"date-time":"2005-03-04T02:30:43Z","timestamp":1109903443000},"page":"603-607","source":"Crossref","is-referenced-by-count":46,"title":["cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1)"],"prefix":"10.1111","volume":"178","author":[{"given":"Wolfgang","family":"GEBHARD","sequence":"first","affiliation":[]},{"given":"Matthias","family":"SCHUBE","sequence":"additional","affiliation":[]},{"given":"Manfred","family":"EULITZ","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2005,3,3]]},"reference":[{"key":"e_1_2_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-2952(62)90119-3"},{"key":"e_1_2_3_3_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI106462"},{"key":"e_1_2_3_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2795(74)90007-5"},{"key":"e_1_2_3_5_2","doi-asserted-by":"crossref","first-page":"3907","DOI":"10.1016\/S0021-9258(17)34776-2","volume":"253","author":"Plummer T. 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