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This paper reports the partial purification and characterization of a new type of arginase from chicken liver. The enzyme can be demonstrated only in less than 10% of a fasting chicken population, and has never been found in fed animals. The new arginase differs with respect to several properties (chromatographic behaviour, sedimentation coefficient, Km for arginne) from the arginase normally found in chicken liver and is more like the ureotelic arginase isolated from rat liver. [ABSTRACT FROM AUTHOR]

The modification of one cysteine residue of transamidinase by reaction with 5,5′-dithiobis-2-nitrobenzoic acid alters the catalytic properties of the enzyme. The Michaelis constant of transamidinase for arginine is increased and the capacity to utilize glycine and hydroxylamine as amidine acceptors is lost. Arginine, the amidine donor substrate, protects the cysteine residue and prevents the changes in catalytic activity induced by the treatment with 5,5′-dithiobis-2-nitrobenzoic acid. [ABSTRACT FROM AUTHOR]

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Copyright of Experientia is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)