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Metabolism and Enzymology

Antipeptide Antibodies That Can Distinguish Specific Subunit Polypeptides of Glutamine Synthetase from Bean (Phaseolus vulgaris L.) ¹

Division of Biology, Ackert Hall, Kansas State University, Manhattan, Kansas 66506

The amino acid sequences of the and subunit polypeptides of glutamine synthetase from bean (Phaseolus vulgaris L.) root nodules are very similar. However, there are small regions within the sequences that are significantly different between the two polypeptides. The sequences between amino acids 2 and 9 and between 264 and 274 are examples. Three peptides (_2-9, _264-274, and _264-274) corresponding to these sequences were synthesized. Antibodies against these peptides were raised in rabbits and purified with corresponding peptide-Sepharose affinity chromatography. Western blot analysis of polyacrylamide gel electrophoresis of bean nodule proteins demonstrated that the anti-_264-274 antibodies reacted specifically with the polypeptide and the anti-_264-274 and anti-_2-9 antibodies reacted specifically with the polypeptide of the native and denatured glutamine synthetase. These results showed the feasibility of using synthetic peptides in developing antibodies that are capable of distinguishing proteins with similar primary structures.