Human urinary kallikrein--amino acid sequence and carbohydrate attachment sites.
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Kellermann J, Lottspeich F, Geiger R, Deutzmann R
Human urinary kallikrein--amino acid sequence and carbohydrate attachment sites.
Protein Seq Data Anal. 1988 Feb;1(3):177-82.
- PubMed ID
- 3163150 [ View in PubMed]
- Abstract
The amino acid sequence of human urinary kallikrein was determined by protein-chemical methods. The peptide chain contains 238 amino acid residues. Ten half-cystine residues form five disulfide bridges. Six carbohydrate side chains could be identified, three of them are N-glycosidically linked to asparagine which is present in the acceptor sequon Asn-Xaa-Thr (or -Ser) and three are O-glycosidically linked to two serine residues and one threonine residue, respectively. Comparison of the primary structure of human urinary kallikrein with that of other serine proteinases especially porcine kallikrein and rat kallikrein shows a high degree of homology. IVGGWECEQHSQPWQAALYHFSTFQCGGILVHRQWVLTA AHCISDNYQLWLGRHNLFDDENTAQFVHVSESFPHPGFN MSLLENHTRQADEDYSHDLMLLRLTEPADTITDAVKVVE LPTQEPEVGSTCLASGWGSIEPENFSFPDDLQCVDLKIL PNDECEKAHVQKVTDFMLCVGHLEGGKDTCVGDSGGPLM CDGVLQGVTSWGYVPCGTPNKPSVAVRVLSYVKWIEDTIAENS.