[Comparison of protein composition and activities of pilose antler processed by different methods].
To elucidate the influence of processing conditions on pilose antlerś therapic effects, the protein composition and activities were compared on three kinds of pilose antler processed by lyophilization, freezing and traditional short-time heating, respectively. The concentration of the water soluble protein in freeze-dried pilose antler was 126.54 mg/g (Folin-Phenol assay), which was 13.1 times higher than that of heating processed antler. These proteins distributed widely in SDS-PAGE electrophoresis and the protein band between 50.0 kDa approximately 60.0 kDa achieved the highest concentration. The water extract of freeze-dried antler promoted the proliferation and IGF-I secretion of rat osteogenic-like cell UMR-106 by 245.25% ( MTT assay) and 66.36 ng/ml, which was respectively 2.2 times and 1.2 times of those of heating processed antler. The same candidate inhibited the growth of human hepatic carcinoma cell BEL-7402 by the highest rate of 47.64% , which was 1.4 times of heating processed antler. The activities of frozen fresh pilose antler were lower than those of its freeze-dried counterpart, but were much higher than those of heating processed antler. The results indicated that lyophilization help to remain the activity of pilose antlerś proteins as much as possible and improve its efficacy.
Ke
Li-jing
LJ
Institute of Biotechnology, Fuzhou University, Fuzhou 350002, China.
Lin
Dong-yun
DY
Huang
Xiao-nan
XN
Huo
Yu-shu
YS
Rao
Ping-fan
PF
Ye
Xiu-yun
XY
D000818:Animals; D000999:Antlers / Q000737:chemistry*; D045744:Cell Line, Tumor; D049109:Cell Proliferation / Q000187:drug effects*; D003670:Deer; D005612:Freeze Drying / Q000379:methods; D006358:Hot Temperature; D006801:Humans; D007334:Insulin-Like Growth Factor I / Q000378:metabolism; D008297:Male; D008419:Materia Medica / Q000302:isolation & purification / Q000494:pharmacology*; D010006:Osteoblasts / Q000378:metabolism / Q000473:pathology; D012516:Osteosarcoma / Q000378:metabolism / Q000473:pathology; D011506:Proteins / Q000032:analysis* / Q000302:isolation & purification; D012709:Serum Albumin / Q000032:analysis / Q000302:isolation & purification; D013678:Technology, Pharmaceutical / Q000379:methods*
D008419:Materia Medica; D011506:Proteins; D012709:Serum Albumin; D007334:Insulin-Like Growth Factor I