The complete amino acid sequence of human urinary kallikrein has been determined. The enzyme was a single polypeptide which comprised 238 amino acid residues. In the case of prokallikrein, a propeptide which was consisted of seven amino acid residues was attached to N-terminal isoleucine of kallikrein. The sequence of Asn-X-Thr(Ser), common to glycosylation site, was identified at positions 78-80, 84-86 and 141-143. It has been shown from the sequence of kallikrein that Arg(-1)-Ile(1) and Arg(87)-Gln(88) bonds are hydrolyzed with trypsin on rapid activation of prokallikrein and the formation of disulfide-linked two chain kallikrein.
CITATION STYLE
Takahashi, S., Irie, A., Katayama, Y., & Miyake, Y. (1989). Human urinary prokallikrein--structural analysis on activation mechanism. Advances in Experimental Medicine and Biology, 247 A, 513–518. https://doi.org/10.1007/978-1-4615-9543-4_79
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