Comparison of Two Lectins Isolated from Xenopus Cortical Granules : Biochemistry
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Two cortical granule lectins (CGLs) of Xenopus laevis were compared by PAGE, immunodiffusion, immunoblot, atomic absorption and amino acid analysis. The CGL was released following activation of coelomic eggs by electric stimuli and purified by affinity chromatography with immobilized melibiose. On PAGE in native condition, the purified CGL existed in two different molecular forms, CGL-1 and CGL-2. The two were isolated electrophoretically from polyacrylamide gel. The CGLs had the following characteristics in common: (1) the specific activity of hemagglutination; (2) the specific binding to galactosides; (3) a calcium requirement; (4) calcium content of 5.69-7.24 mole per 10^5g protein, and (5) antigenicity to an antiserum raised against CGL-1. Differing characteristics included: (1) the molecular weights of the subunits (42kDa and 46kDa for CGL-1, and 39-46kDa for CGL-2); (2) the pI value of the native lectins (4.55 for CGL-1 and 4.70 for CGL-2); (3) the isofocusing pattern of the subunits, and (4) the amino acid composition, such that the amount of tyrosine is less but that of valin and tryptophan greater in CGL-2 than in CGL-1. So CGL-1 and CGL-2 differ in their particular combination of subunits, each of which is heterogeneous in size, charge and amino acid sequence.
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