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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Published in | Journal of investigative dermatology Vol. 67; no. 5; pp. 582 - 586 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
01.11.1976
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Subjects | |
Online Access | Get full text |
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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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0022-202X 1523-1747 |
DOI: | 10.1111/1523-1747.ep12541685 |