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J. Biochem, 1988, Vol. 104, No. 1 22-29
© 1988 Japanese Biochemical Society

research-article

Primary Structure of Human Urinary Prokallikrein1

Saori Takashashi*, Akiko Irie** and Yoshihiro Miyake*,2

Department of Biochemistry, National Cardiovascular Center Research Institute Suita,Osaka 565

2 To whom correspondence should be addressed

The complete amino acid sequence of human urinary prokallikrein has been determined by amino acid analysis and sequence determination of peptide fragments obtained from chemical and enzymological cleavages of kallikreinand by comparison of the N-terminal sequence of prokallikrein with that of kallikrein, the active form. Prokallikrein was a single chain polypeptide which comprised 238 amino acid residues of kallikrein and 7 amino acid residues of the propeptide. The sequence, Asn-X-Thr(Ser), which is a common glycosylation site was found at positions 78–80, 84–86, and 141–143. Two trypsin-susceptible sites were identified. One is the Arg(-1)-Ile(1) bond and the other is the Arg (87)-Gln(88) bond. The sequence of human urinary kallikrein was identical with that of human pancreatic and kidney kallikreins (Fukushima, D. et al. (1985) Biochemistry 24, 8037–8043; Baker, A.R. & Shine, J. (1985) DNA 4, 445–459), which were predicted from the nucleotide sequences of cDNAs. The primary structure of human urinary kallikrein is homologous to those of the other animal kallikreins and kallikrein-related proteins. Key amino acid residues, His(41), Asp(96), and Ser(190), required for catalytic activity and Asp (184) required for kallikrein-type specificity are completely conserved. The results show that human urinary prokallikrein and kallikrein are of tissue type and they are excreted in urine without any modification.

1 Preliminary results have been presented at the 5th International Congress on Kininheld in Tokyo, Nov. 29-Dec. 3, 1987. This work was supported in part by Grants-in-Aid for Special Project Research (No. 62122005) and for Scientific Research (No. 61570151) from the Ministry of Education, Science and Culture of Japan.


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