Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1991 Apr 15;275(Pt 2):541–543. doi: 10.1042/bj2750541

Purification and characterization of truncated ribonuclease inhibitor.

J Hofsteenge 1, A Vincentini 1, S R Stone 1
PMCID: PMC1150084  PMID: 2025233

Abstract

A recombinant pig ribonuclease inhibitor (delta r-RI) lacking 90 or 93 N-terminal amino acid residues was isolated from a preparation of recombinant inhibitor. The kinetic parameters for the inhibition of ribonuclease A by delta r-RI were determined and found to be only slightly altered in comparison with the full-length inhibitor. The deletion did, however, affect the surface properties of RI. The results are discussed in relation to those obtained by Lee & Vallee [(1990) Proc. Natl. Acad. Sci. U.S.A. 87, 1879-1883].

Full text

PDF
541

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Blackburn P., Wilson G., Moore S. Ribonuclease inhibitor from human placenta. Purification and properties. J Biol Chem. 1977 Aug 25;252(16):5904–5910. [PubMed] [Google Scholar]
  2. Hinnen A., Hicks J. B., Fink G. R. Transformation of yeast. Proc Natl Acad Sci U S A. 1978 Apr;75(4):1929–1933. doi: 10.1073/pnas.75.4.1929. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Hofsteenge J., Kieffer B., Matthies R., Hemmings B. A., Stone S. R. Amino acid sequence of the ribonuclease inhibitor from porcine liver reveals the presence of leucine-rich repeats. Biochemistry. 1988 Nov 15;27(23):8537–8544. doi: 10.1021/bi00423a006. [DOI] [PubMed] [Google Scholar]
  4. Lee F. S., Fox E. A., Zhou H. M., Strydom D. J., Vallee B. L. Primary structure of human placental ribonuclease inhibitor. Biochemistry. 1988 Nov 15;27(23):8545–8553. doi: 10.1021/bi00423a007. [DOI] [PubMed] [Google Scholar]
  5. Lee F. S., Shapiro R., Vallee B. L. Tight-binding inhibition of angiogenin and ribonuclease A by placental ribonuclease inhibitor. Biochemistry. 1989 Jan 10;28(1):225–230. doi: 10.1021/bi00427a031. [DOI] [PubMed] [Google Scholar]
  6. Lee F. S., Vallee B. L. Kinetic characterization of two active mutants of placental ribonuclease inhibitor that lack internal repeats. Biochemistry. 1990 Jul 17;29(28):6633–6638. doi: 10.1021/bi00480a012. [DOI] [PubMed] [Google Scholar]
  7. Lee F. S., Vallee B. L. Modular mutagenesis of human placental ribonuclease inhibitor, a protein with leucine-rich repeats. Proc Natl Acad Sci U S A. 1990 Mar;87(5):1879–1883. doi: 10.1073/pnas.87.5.1879. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Morrison J. F., Walsh C. T. The behavior and significance of slow-binding enzyme inhibitors. Adv Enzymol Relat Areas Mol Biol. 1988;61:201–301. doi: 10.1002/9780470123072.ch5. [DOI] [PubMed] [Google Scholar]
  9. ROTH J. S. Ribonuclease. VII. Partial purification and characterization of a ribonuclease inhibitor in rat liver supernatant fraction. J Biol Chem. 1958 Apr;231(2):1085–1095. [PubMed] [Google Scholar]
  10. SHORTMAN K. Studies on cellular inhibitors of ribonuclease. II. Some properties of the inhibitor from rat liver. Biochim Biophys Acta. 1962 Jan 22;55:88–96. doi: 10.1016/0006-3002(62)90934-4. [DOI] [PubMed] [Google Scholar]
  11. Schneider R., Schneider-Scherzer E., Thurnher M., Auer B., Schweiger M. The primary structure of human ribonuclease/angiogenin inhibitor (RAI) discloses a novel highly diversified protein superfamily with a common repetitive module. EMBO J. 1988 Dec 20;7(13):4151–4156. doi: 10.1002/j.1460-2075.1988.tb03310.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Stone S. R., Hofsteenge J. Kinetics of the inhibition of thrombin by hirudin. Biochemistry. 1986 Aug 12;25(16):4622–4628. doi: 10.1021/bi00364a025. [DOI] [PubMed] [Google Scholar]
  13. Vicentini A. M., Kieffer B., Matthies R., Meyhack B., Hemmings B. A., Stone S. R., Hofsteenge J. Protein chemical and kinetic characterization of recombinant porcine ribonuclease inhibitor expressed in Saccharomyces cerevisiae. Biochemistry. 1990 Sep 18;29(37):8827–8834. doi: 10.1021/bi00489a046. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES