Primary structure of hemocyanin subunit c from Panulirus interruptus.
The amino acid sequence of the hemocyanin subunit c from the spiny lobster, Panulirus interruptus, has been determined. The elucidation was mainly based on three digests, with CNBr, trypsin and endoproteinase Glu-C, respectively. Additional evidence was obtained by sequencing of peptides from an endoproteinase Lys-C digest. Subunit c is a polypeptide with 661 amino acid residues and with a carbohydrate group attached to residue 476 in the third domain. No heterogeneity was observed. The degree of identity with subunit a is 59%. Some differences with subunit a are an N-terminal extension of six residues, a one-residue C-terminal extension, and a three-residue deletion. Furthermore, carbohydrate attachment is in a different position, as are most half-cystine residues. Limited trypsinolysis resulted in cleavage at the same site as in subunits a and b.
Neuteboom
B
B
Biochemisch Laboratorium, Rijksuniversiteit Groningen, The Netherlands.
Jekel
P A
PA
Beintema
J J
JJ
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D002241:Carbohydrates / Q000032:analysis; D003488:Cyanogen Bromide; D006433:Hemocyanins / Q000737:chemistry* / Q000235:genetics; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D005810:Multigene Family; D008121:Nephropidae; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D014357:Trypsin
D002241:Carbohydrates; D046911:Macromolecular Substances; D010446:Peptide Fragments; D006433:Hemocyanins; D014357:Trypsin; D003488:Cyanogen Bromide