A 20-kDa protein with the GTP-binding and trypsin inhibitory activities from Glycine max.
A 20-kDa protein (p20) with a GTP binding activity was purified from the cultured cells of Glycine max (soybean). The amino acid sequence of p20 showed 65% identity in a 23 amino acid overlap against the Kunitz-type trypsin inhibitor of soybean reported. Furthermore, it was found that a Kunitz-type soybean trypsin inhibitor of commercial origin also binds GTP.
Hirata
T
T
Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Japan. thirata@sci.hiroshima-u.ac.jp
Izumi
S
S
Tsuji
S
S
D000595:Amino Acid Sequence; D002478:Cells, Cultured; D019204:GTP-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology; D006160:Guanosine Triphosphate / Q000378:metabolism*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D013025:Glycine max / Q000737:chemistry*; D014361:Trypsin Inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology
D014361:Trypsin Inhibitors; D006160:Guanosine Triphosphate; D019204:GTP-Binding Proteins