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Identification of [hydroxyproline 3 ]‐lysyl‐bradykinin released from human kininogens by human urinary kallikrein
Author(s) -
Maier Manfred,
Reissert Guenther,
Jerabek Ingrid,
Lottspeich F.,
Binder Bernd R.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80778-6
Subject(s) - bradykinin , kinin , kallikrein , hydroxylation , chemistry , biochemistry , hydroxyproline , bioassay , biological activity , enzyme , chromatography , in vitro , biology , receptor , genetics
The types of kinins released from purified native, single chain human high and low molecular mass kininogens (HMMKs and LMMKS, respectively) by purified human urinary kallikrein were separated by reverse‐phase HPLC and quantitated by the rat uterus bioassay. [Hyp 3 ]‐ysyl‐bradykinin, a recently discovered kinin, represented up to 58% of the biological activity released from 4 individual HMMK preparations purified from 4 different healthy volunteers. In contrast, the majority of the biological activity released from LMMKs purified from pooled plasma was identified as Lys‐bradykinin and [Hyp 3 ]‐lysyl‐bradykinin represented only 6.4 ± 3.8%. These findings indicate posttranslational hydroxylation of human kininogens and suggest a preference of HMMKs for this modification.