Purification and crystallization of the polypeptide hormone human chorionic somatomammotropin.
作者： R.E. Hunt , K. Moffat , D.W. Golde
DOI: 10.1016/S0021-9258(19)69096-4
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摘要: Abstract We have purified the large polypeptide hormone human chorionic somatomammotropin to near electrophoretic homogeneity by a new purification scheme. The crystallized from polyethylene glycol in form suitable for high resolution x-ray analysis; crystals are monoclinic, space group C2, = 123.9, b 30.3, c 53.8 A, beta 119 degrees 30 min, with 1 molecule/asymmetric unit. growth-promoting activity of homogeneous and dissolved was measured through their effect on committed erythroid precursor cells tissue culture assays. Both redissolved crystalline had activities comparable that standard procedures. latter preparations yielded either no crystals, or disordered unsuitable analysis.
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