Partial amino acid sequence of a hemocyanin subunit from Palinurus vulgaris.
1. Hemocyanin from the spiny lobster Palinurus vulgaris was separated into two fractions, which were designated as subunits a and b. 2. 55% of the amino acid sequence of subunit b has been determined. A comparison with Panulirus interruptus hemocyanins shows 78% sequence identity with subunit a and 56% with subunit c. It has carbohydrate attached to domain one. Two half-cystines have been substituted, indicating that it probably possesses only one disulfide bridge. Heterogeneity has been observed in seven out of 380 positions determined so far. 3. Subunit a is almost identical with subunit b. In contrast to Panulirus interruptus and Panulirus japonicus, Palinurus vulgaris hemocyanin contains no c-type subunit. 4. A position in the tentative evolutionary tree of arthropod hemocyanins based on sequence differences has been assigned to Palinurus vulgaris subunit b.
Neuteboom
B
B
Biochemisch Laboratorium, Rijksuniversiteit Groningen, The Netherlands.
Dokter
W
W
van Gijsen
J
J
Rensink
H
H
de Vries
J
J
Beintema
J J
JJ
D000595:Amino Acid Sequence; D000818:Animals; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006433:Hemocyanins / Q000032:analysis*; D008969:Molecular Sequence Data; D008121:Nephropidae / Q000378:metabolism*
D006433:Hemocyanins