Partially hydrolized ribonuclease with enzymic activity

Rogers, William I.; Kalnitsky, George

doi:10.1016/0006-3002(57)90372-4

Cited by 20 publications

(2 citation statements)

References 32 publications

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“…Several other workers have reported differences in the specificities of RNase toward its substrates, after various alterations of the RNase molecule (van Vunakis et al, 1960; Kalman et al, 1955;Nelson and Hummel, 1961). Their results, as well as the present disparities, could be explained by a preferential attack on one of two active centers (Rogers and Kalnitsky, 1957) or on one of two binding sites.…”

Section: Discussionmentioning

confidence: 63%

The Thiolation of Ribonuclease

White¹,

Sandoval²

1962

Biochemistry

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The thiolating agent, N-acetyl homocysteine thiolactone, reacts with the primary amino groups of proteins to introduce the A'-acetyl homocysteinyl residue. The appearance of sulfhydryl groups during the thiolation of ribonuclease, as well as of S-carboxymethylhomocysteinyl and S-carboxymethyleysteinyl residues after reaction of the thiolated protein with iodoacetate, indicated close to three N-acetyl homocysteinyl residues added per average molecule of protein after prolonged reaction. Chromatographic examination on CM-cellulose, however, showed the presence of a slow-forming component containing five .ZV-acetyl homocysteinyl residues, while other components were less ex-

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