Purification and characterization of truncated ribonuclease inhibitor.
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].
Hofsteenge
J
J
Friedrich Miescher-Institut, Basel, Switzerland.
Vincentini
A
A
Stone
S R
SR
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D047908:Intracellular Signaling Peptides and Proteins; D007700:Kinetics; D010446:Peptide Fragments / Q000235:genetics / Q000302:isolation & purification* / Q000494:pharmacology; D011485:Protein Binding; D011506:Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000494:pharmacology; D011994:Recombinant Proteins / Q000378:metabolism / Q000494:pharmacology; D012259:Ribonuclease, Pancreatic / Q000037:antagonists & inhibitors*; D012441:Saccharomyces cerevisiae / Q000235:genetics; D013552:Swine
D000596:Amino Acids; D047908:Intracellular Signaling Peptides and Proteins; D010446:Peptide Fragments; D011506:Proteins; D011994:Recombinant Proteins; C066953:ribonuclease inhibitor, porcine; D012259:Ribonuclease, Pancreatic