Analysis of the interactions of human ribonuclease inhibitor with angiogenin and ribonuclease A by mutagenesis: importance of inhibitor residues inside versus outside the C-terminal “hot spot” 1 1Edited by J. Wells

2000 ◽  
Vol 302 (2) ◽  
pp. 497-519 ◽  
Author(s):  
Robert Shapiro ◽  
Melisa Ruiz-Gutierrez ◽  
Chang-Zheng Chen
Keyword(s):  
Hot Spot ◽  
Ribonuclease A ◽  
Ribonuclease Inhibitor

scholarly journals Thiol-Disulfide Exchange of Ribonuclease Inhibitor Bound to Ribonuclease A EVIDENCE OF ACTIVE INHIBITOR-BOUND RIBONUCLEASE

1995 ◽  
Vol 270 (48) ◽  
pp. 28570-28578 ◽  
Author(s):  
Mercedes Ferreras ◽  
José G. Gavilanes ◽  
Carlos López-Otín ◽  
Juan M. García-Segura
Keyword(s):  
Ribonuclease A ◽  
Ribonuclease Inhibitor ◽  
Active Inhibitor ◽  
Disulfide Exchange

Fluorescence Assay for the Binding of Ribonuclease A to the Ribonuclease Inhibitor Protein

2002 ◽  
Vol 306 (1) ◽  
pp. 100-107 ◽  
Author(s):  
Richele L. Abel ◽  
Marcia C. Haigis ◽  
Chiwook Park ◽  
Ronald T. Raines
Keyword(s):  
Ribonuclease A ◽  
Fluorescence Assay ◽  
Inhibitor Protein ◽  
Ribonuclease Inhibitor

scholarly journals Purification and characterization of truncated ribonuclease inhibitor

1991 ◽  
Vol 275 (2) ◽  
pp. 541-543 ◽  
Author(s):  
J Hofsteenge ◽  
A Vincentini ◽  
S R Stone
Keyword(s):  
Amino Acid ◽  
Kinetic Parameters ◽  
Surface Properties ◽  
Ribonuclease A ◽  
Amino Acid Residues ◽  
Ribonuclease Inhibitor ◽  
Purification And Characterization ◽  
Terminal Amino Acid ◽  
Terminal Amino

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].

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