Heterogeneity in buffalo lutropin.

ABSTRACT

Lutropin (LH-1) from water buffaloes has been shown to exhibit microheterogeneity in the N-terminal amino-acid sequence of its alpha-subunit. The beta-subunit did not exhibit such microheterogeneity. Another protocol of purification yielded a preparation of buffalo LH (bu LH-2) different from the buffalo LH-1 in certain physico-chemical properties like ease of dissociation into subunits, sugar composition, isoelectric point, and elution profile on S-200. Data appear to indicate the presence of more than one form of buffalo lutropin.