1970 Volume 34 Issue 1 Pages 61-67
The molecular weight of γ1 globulin was determined as 2.0 × 105 by the Archibald method, and the intrinsic viscosity, [η], and the sedimentation coefficient, s°20, w, were found to be 0.0424dl/g and 7.26S respectively. These values indicated the large asymmetry of the protein. The protein was composed of 18 residues of hexose, 3 residues of pentose, 6 residues of hexosamine and 1751 residues of amino acids: Lys58, His47, Arg148, Asp126, Glu273, Gly161, Ala144, Val121, Leu106, Ile72, Pro83, Ser136, Thr48, Hyp68, Cys17, Met16, Tyr44, Trp8, Phe75 and amide ammonia163. The N-terminal amino acid analysis suggested that the protein was composed of ten subunits. The properties and the composition were discussed in comparison with those of the 7S globulin of soybean cotyledon.
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