[Extraction, purification and identification of type II collagen from Agkistrodon acutus].
The object of the research was to extract, purify and identify the type II collagen of Agkistrodon acutus. Type II collagen of A. acutus was extracted by enzyme decomposition method, and purified by ion exchange column chromatography. It was characterized by SDS-PAGE gel electrophoresis, ultraviolet spectrophotometry, infrared absorption spectroscopy and mass spectroscopy. The results showed that the size of C II was about 130 kDa. It absorbed at 223 nm. IR spectrum obtained showed that the triple helical domains of amino-acid sequences were characterized by the repetition of triplets Gly-X-Y. The MS spectrum graphically stated that C II extracted from cow and A. acutus have the similar peptides. The C II of A. acutus was obtained by extraction and purification. Appraisal analysis by SDS-PAGE, UV, IR and MS, C II of A. acutus was consistent with the standard C II of cow. It was proved that the extracted protein was C II.
Zhejiang Chinese Medical University, Hangzhou 310053, China.
Heng-Cun
HC
Gu
Zhejiang Chinese Medical University, Hangzhou 310053, China.
Jin-Bo
JB
Hu
Zhejiang Chinese Medical University, Hangzhou 310053, China.
Zhi-Shan
ZS
Ding
Zhejiang Chinese Medical University, Hangzhou 310053, China.
Yong-Sheng
YS
Fan
Zhejiang Chinese Medical University, Hangzhou 310053, China.
Xing-Hong
XH
Ding
D017836:Agkistrodon / Q000378:metabolism*; D000818:Animals; D024043:Collagen Type II / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D013058:Mass Spectrometry; D030162:Reptilian Proteins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism
D024043:Collagen Type II; D030162:Reptilian Proteins