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KMID : 0578319910010020177
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Molecules and Cells
1991 Volume.1 No. 2 p.177 ~ p.182
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Purification and characterization of Myoblast fusion Inhibitor Chick Embryo Extract
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Lee, Do Hee
Kwak, Kyu Bong/Park, Young Chul/Chung, Chin Ha/Ha, Doo Bong
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Abstract
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A protein capable of inhibiting myoblast fusion was purified to homogeniety from chick embryo extracts using conventional chromatographic procedures. This inhibitor protein has an apparent molecular weight of 67 kDa as determined by gel filtration on a Sephacryl S-200 column. It has isoelectric point of 7.1. When the purified inhibitor was run on the SDS-polyacrylamide gel electrophoresis. it was separated into two bands with sizes of 30 and 32 kDa. The smaller molecular weight species appeared to be generated from the larger protein, since the hydrolysis of the bands using S. aureus V8 protease yielded a similar pattern of the digested products upon the second gel electrophoresis. The inhibitory effect of the purified protein can be seen at a concentration as low as 4 g/ml, and is maximal at 30 gg/ml. However, little or no effect was observed on the proliferation of the cultured myoblasts at the inhibitors concentrations tested. Thus, the purified 67-kDa protein appeared to be capable of blocking myoblast fusion without affecting the cell proliferation. These results suggest that the 67-kDa protein may play an important role in the regulation of myogenic differentiation through its ability to control myoblast fusion.
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