Isoenzymatic forms alpha 2, alpha beta, and beta 2 of bovine seminal ribonuclease are generated by the transformation of beta-type into alpha-type subunit through deamidation of a single amide group [Di Donato, A., & D'Alessio, G. (1981) Biochemistry 20, 7232-7237]. The residue involved in this selective deamidation has been identified as Asn67. Deamidation occurs by formation of a cyclic imide intermediate involving the Gly at position 68. Opening of the cyclic imide may occur on either side of the nitrogen, generating both the normal alpha-aspartyl and an isoaspartyl residue at position 67. The alpha-carboxyl of the isoaspartyl residue is effectively methylated by bovine brain protein carboxylmethyltransferase.