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 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.
D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D001120:Arginine / Q000378:metabolism*; D006168:Guinea Pigs; D006197:Hair; D012867:Skin / Q000201:enzymology*
D001120:Arginine; D000217:Acyltransferases