Structural difference between the two forms of guinea-pig beta 2-microglobulin and their occurrence in inbred guinea-pig strains |
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Authors: | R Cigén |
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Affiliation: | Department of Physiological Chemistry, University of Lund, P.O. Box 94, S-221 00 Lund, Sweden |
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Abstract: | The structural difference between two forms (basic and acidic) of guinea-pig beta 2-microglobulin (beta 2m) has been established. Both forms are present in urine from inbred guinea-pig strains. The beta 2m forms were each digested with carboxypeptidase Y and carboxypeptidase A contaminated with carboxypeptidase B. Released amino acids were separated from remaining protein, dansylated and analysed by 2-dimensional TLC on polyamide layer sheets. From the results it was concluded that the basic beta 2m form has lysine and the acidic beta 2m form has asparagine as their respective C-terminal amino acids. The acidic form is also 1 amino acid (lysine) shorter than the basic form, which is supported by electrophoretic studies on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The presence of the 2 forms of beta 2m in urine from inbred guinea-pig strains 2 and 13, shown by gel filtration and ion exchange chromatography, makes it unlikely that the 2 forms are a result of genetic polymorphism. |
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Keywords: | CPA carboxypeptidase A CPB carboxypeptidase B CPA/B CPA contaminated with CPB CPY carboxypeptidase Y DFP diisopropylphosphofluoridate DNS-C1 5-dimethylamino-1-naphthalenesulfonyl-chloride PMSF phenylmethylsulfonylfluoride SDS sodium dodecyl sulfate SDS-PAGE SDS-polyacrylamide gel electrophoresis |
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