Identification of [hydroxyproline3]‐lysyl‐bradykinin released from human kininogens by human urinary kallikrein
- 23 May 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 232 (2) , 395-398
- https://doi.org/10.1016/0014-5793(88)80778-6
Abstract
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. [Hyp3]‐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 [Hyp3]‐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.Keywords
This publication has 19 references indexed in Scilit:
- Identification of [Hydroxyproline3]-lysyl-bradykinin released from human plasma protein by kallikreinBiochemical and Biophysical Research Communications, 1988
- Human high molecular weight kininogen as a thiol proteinase inhibitor: presence of the entire inhibition capacity in the native form of heavy chainBiochemistry, 1986
- Human Ile-Ser-Bradykinin, Identical with Rat T-Kinin, is a Major Permeability Factor in Ovarian Carcinoma AscitesBiological Chemistry Hoppe-Seyler, 1986
- Microscale isocratic separation of phenylthiohydantoin amino acid derivativesJournal of Chromatography A, 1985
- Human plasma kininogens are identical with α‐cysteine proteinase inhibitorsFEBS Letters, 1985
- Isolation of a human cDNA for .alpha.2-thiol proteinase inhibitor and its identity with low molecular weight kininogenBiochemistry, 1984
- Kinins are generated in vivo following nasal airway challenge of allergic individuals with allergen.Journal of Clinical Investigation, 1983
- Identification of the Phenylthiohydantoin Derivatives of Amino Acids by High Pressure Liquid Chromatography, Using a Ternary, Isocratic Solvent SystemHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1980
- The Biosynthesis of Collagen and Its DisordersNew England Journal of Medicine, 1979
- Substrate specificity of collagen proline hydroxylase: Hydroxylation of a specific proline residue in bradykininArchives of Biochemistry and Biophysics, 1969