Comparative characterization of hyperglycemic neuropeptides from the lobster Homarus americanus.
With the use of a two-step HPLC purification procedure, two sets of two isoforms of the crustacean hyperglycemic hormone (CHH) were isolated from sinus glands of the lobster Homarus americanus. Structural differences between the two groups of isoforms were found in their amino acid sequences, amino acid compositions and precise molecular weights. Using peptide mapping, the difference between the isoforms in each group was located within the first eight amino acids at the N-termini. The nature of this difference remained unclear as all four peptides had the same N-terminal amino acid sequence unto residue 19.
Tensen
C P
CP
Department of Experimental Zoology, Faculty of Sciences, Catholic University of Nijmegen, The Netherlands.
Janssen
K P
KP
Soyez
D
D
Van Herp
F
F
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006943:Hyperglycemia / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D008121:Nephropidae / Q000378:metabolism*; D009479:Neuropeptides / Q000737:chemistry / Q000302:isolation & purification*; D010449:Peptide Mapping; D012689:Sequence Homology, Nucleic Acid; D016339:Spectrometry, Mass, Fast Atom Bombardment
D000596:Amino Acids; D009479:Neuropeptides