Literature DB >> 3924907

A study on renin binding protein (RnBP) in the human kidney.

S Takahashi, R Miura, Y Miyake.   

Abstract

We purified, from human kidney, a protein that reacts with rabbit anti-porcine kidney renin binding protein (RnBP) antiserum by trapping with porcine kidney renin. The purified preparation showed a single protein peak on gel filtration by high performance liquid chromatography (HPLC) and two protein bands on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The latter two kinds of protein were identified as the porcine renin and human kidney protein from their electrophoretic mobilities and reactivity toward rabbit anti-porcine kidney renin and RnBP antisera. The molecular weights of the purified preparation and the human kidney protein were estimated to be 56,000 by HPLC and 43,000 by SDS-PAGE, respectively. The specific activity of porcine renin in the purified preparation was 8.6 mg angiotensin I per mg of protein per h at 37 degrees C and pH 6.5. This specific activity was about one-fifth that of free porcine renin. Therefore, it is suggested from the reactivity toward the anti-porcine RnBP antiserum and inhibitory action toward porcine renin that the human kidney protein is RnBP and that the human RnBP is purified as a complex with porcine renin.

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Year:  1985        PMID: 3924907     DOI: 10.1093/oxfordjournals.jbchem.a135103

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  1 in total

1.  Renin and angiotensinogen expression and functions in growth and apoptosis of human glioblastoma.

Authors:  L Juillerat-Jeanneret; J Celerier; C Chapuis Bernasconi; G Nguyen; W Wostl; H P Maerki; R-C Janzer; P Corvol; J-M Gasc
Journal:  Br J Cancer       Date:  2004-03-08       Impact factor: 7.640

  1 in total

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