Arginine Transferase Activity In Homogenates From Guinea-Pig Hair Follicles

The transfer of arginine from tRNA to the amino terminal region of acceptor proteins has been demonstrated in postribosomal supernatant from guinea-pig hair follicle homogenate. The reaction has no requirement for template nucleic acids, ATP, GTP, or Mg++, and is unaffected by high concentrations of...

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Bibliographic Details
Published inJournal of investigative dermatology Vol. 67; no. 5; pp. 582 - 586
Main Authors Lock, Robert A., Harding, Harry W.J., Rogers, George E.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.11.1976
Subjects
Acyltransferases - metabolism
Animals
Arginine - metabolism
Guinea Pigs
Hair
Skin - enzymology
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Summary:The transfer of arginine from tRNA to the amino terminal region of acceptor proteins has been demonstrated in postribosomal supernatant from guinea-pig hair follicle homogenate. The reaction has no requirement for template nucleic acids, ATP, GTP, or Mg++, and is unaffected by high concentrations of cycloheximide. It is concluded that the arginine transfer activity of the guinea-pig hair follicle is due to the action of a soluble enzyme similar to the arginine transferases previously described for other mammalian tissues.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0022-202X
1523-1747
DOI:10.1111/1523-1747.ep12541685