This study is a descriptive exploratory study with laboratory observations were conducted in November-December 2015. Analysis of the protein using crude protein transmembrane protein isolated spermatozoa Aberdeen angus beef which is then analyzed using SDS-PAGE electrophoresis method that has led to specific protein bands with heavy 64 kDa molecule as a calcium binding protein and 33 kDa as protein tyrosine phosphorylation. The ribbon is then cut and performed analysis, with methods of electroelution. Protein electroelution calculation result to find that react ATP and phosphorylation activity unit. The results obtained, the protein molecular weight 64 kDa disfosforilasi ATP at 41 ppm with 119,013062x103 activity unit mol / ml / min and a protein with a molecular weight of 33 kDa was phosphorylate ATP by 27 ppm with 78,374456x103 activity unit mol / ml / min. The large amount of ATP that is phosphorylated indicates increasing unit fosoforilasi activity and increased speed phosphorylate proteins in protein.
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