Primary structure of two isoforms of the vitellogenesis inhibiting hormone from the lobster Homarus americanus.

ABSTRACT

The amino acid sequence of two isoforms of the Vitellogenesis Inhibiting Hormone from the lobster Homarus americanus (one biologically active and one inactive in a heterologous bioassay) has been established by gas-phase microsequencing and fast-atom bombardment mass spectrometry. These two isoforms, isolated from sinus glands display the same sequence of 77 amino acid residues (m.w. 9135 Da) and have a free N-terminus. Structurally related to Crustacean Hyperglycemic Hormone and Molt Inhibiting Hormone, the Vitellogenesis Inhibiting Hormone of the lobster clearly appears as an original member of the newly described family of neuropeptides, so far proper to crustaceans, which are involved in the control of major physiological functions.