Regeneration of ribonuclease A from the reduced protein. 1. Conformational analysis of the intermediates by measurements of enzymic activity, optical density, and optical rotation

Biochemistry ◽  
1980 ◽  
Vol 19 (7) ◽  
pp. 1308-1316 ◽  
Author(s):  
Yasuo Konishi ◽  
Harold A. Scheraga
Keyword(s):  
Conformational Analysis ◽  
Optical Density ◽  
Optical Rotation ◽  
Ribonuclease A ◽  
Enzymic Activity

scholarly journals The effect of surfactant structure on ribonuclease A–surfactant interactions

1973 ◽  
Vol 135 (3) ◽  
pp. 547-549 ◽  
Author(s):  
Cecilia Blinkhorn ◽  
Malcolm N. Jones
Keyword(s):  
Anionic Surfactant ◽  
Cationic Surfactants ◽  
Ribonuclease A ◽  
Enzymic Activity ◽  
Head Groups ◽  
Surfactant Interactions ◽  
Dodecylamine Hydrochloride

The enzymic activity of ribonuclease A was measured in the presence of several surfactants at pH7.2. Cationic surfactants with trimethylammonium and pyridinium head groups do not deactivate or denature the enzyme, whereas n-dodecylamine hydrochloride, like the anionic surfactant sodium n-dodecyl sulphate, deactivates and denatures ribonuclease A.

scholarly journals Glycosylation of ribonuclease A catalysed by rabbit liver extracts

1975 ◽  
Vol 146 (2) ◽  
pp. 299-307 ◽  
Author(s):  
Z Khalkhall ◽  
R D Marshall
Keyword(s):  
Metal Ion ◽  
Ribonuclease A ◽  
Enzymic Activity ◽  
Rabbit Liver ◽  
Absolute Requirement ◽  
Pancreatic Ribonuclease A ◽  
Triton X ◽  
Increased Activity ◽  
Asparagine Residue

Crude extracts of rabbit liver catalyse in vitro the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to bovine pancreatic ribonuclease A. The enzymic activity is contained in rough endoplasmic reticulum. It has an absolute requirement for a bivalent metal ion: Co-2+ greater than Mn-2+ greater than Ni-2+. Mg-2+ is ineffective. There is enzymic activity in the absence of detergent, but increased activity is observed in the presence of Triton X-100. The site of glycosylation of ribonuclease A is asparagine-34, and glycosylation occurs only at this point. These findings agree with the hypothesis that the sequence Asn-X-Thr(Ser) (where X may be one of a number of types of amino acid) is a necessary, but not sufficient, condition for N-acetylglucosaminylation of a protein-bound asparagine residue.

Chain-folding initiation structures in ribonuclease A: conformational analysis of trans-Ac-Asn-Pro-Tyr-NHMe and trans-Ac-Tyr-Pro-Asn-NHMe in water and in the solid state

1984 ◽  
Vol 106 (25) ◽  
pp. 7959-7969 ◽  
Author(s):  
G. T. Montelione ◽  
E. Arnold ◽  
Y. C. Meinwald ◽  
E. R. Stimson ◽  
J. B. Denton ◽  
...  
Keyword(s):  
Solid State ◽  
Conformational Analysis ◽  
Ribonuclease A ◽  
Chain Folding
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