Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.26.9 (ribonuclease)
 6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The X-ray structure of the ribonuclease inhibitor from porcine pancreas shows a remarkable non-globular fold. It possesses a large central hole that forms part of the RNase A binding site.
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PMID:'Holy' proteins. I: Ribonuclease inhibitor. 771 83

Four new basic proteins were isolated from horse eosinophils and purified. The eosinophils release these proteins after permeabilization with saponin and degranulation stimulized by guanosine 5'-O-thiotriphosphate. The proteins were separated and purified on a Superose P12- and a Mono S-column by fast protein liquid chromatography. The amino acid composition, the relative molecular mass, the isoelectric point and the partial N-terminal sequence of the four proteins were determined. Papain-activation and ribonuclease activity of the four proteins were tested for comparison with the human eosinophil basic granular proteins. The cytotoxicity of the hole granular extract and of the isolated basic proteins against Escherichia coli K12 was also studied.
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PMID:Isolation and characterization of four basic proteins from horse eosinophilic granules. 848 50

Spectral diffusion dynamics in ribonuclease A was observed via the broadening of photochemical holes burned into the absorption spectrum of intrinsic tyrosine residues. Unlike previous results based on hole burning of chromophores in the pockets of heme proteins, where spectral diffusion develops according to a power law in time, the dynamics in ribonuclease follow a logarithmic law. The results suggest that the experiment preferentially labels the tyrosines located on the surface of the protein where the two-level system dynamics of the glass host matrix exert a strong influence.
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PMID:Investigation of spectral diffusion in ribonuclease by photolabeling of intrinsic aromatic amino acids. 1712 56