Panulirus interruptus hemocyanin. The amino acid sequence of subunit b and anomalous behaviour of subunits a and b on polyacrylamide gel electrophoresis in the presence of SDS.
The primary structure of subunit b of Panulirus interruptus hemocyanin has been derived from two digests (trypsin and CNBr) and, in some cases, with aid from the similarity with the sequence of subunit a. Differences between the amidation states of Asx and Glx residues in subunit b relative to a were investigated more thoroughly. When compared to the sequence of subunit a, 18 differences (2.7%) were found and certain heterogeneities, indicating the presence of a minor subunit b', were observed. Several differences in properties between subunits a and b, including their anomalous behaviour on SDS/polyacrylamide gel electrophoresis, could be explained by amino acid replacements.
Jekel
P A
PA
Biochemisch Laboratorium, Rijksuniversiteit Groningen, The Netherlands.
Bak
H J
HJ
Soeter
N M
NM
Vereijken
J M
JM
Beintema
J J
JJ
D000595:Amino Acid Sequence; D000818:Animals; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D006433:Hemocyanins / Q000235:genetics*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D008121:Nephropidae; D010446:Peptide Fragments / Q000235:genetics; D014357:Trypsin
D010446:Peptide Fragments; D006433:Hemocyanins; D014357:Trypsin; D003488:Cyanogen Bromide