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The complete primary structure of subunit d of the hemocyanin from the tarantula Eurypelma californicum was determined by manual micro sequencing. Subunit d of Mr = 73000 is split about in the middle of the chain during limited trypsinolysis, only one single bond being attacked. The whole chain contains 14 methionine residues and after cyanogen bromide cleavage 15 peptides could be isolated by gel and ion exchange chromatography and high pressure liquid chromatography. The cyanogen bromide peptides and the large (Mr = 34000 and 37000, respectively) fragments resulting from limited trypsinolysis, were further cleaved with trypsin, chymotrypsin, Staphylococcus aureus proteinase, formic acid, and Astacus fluviatilis proteinase, the latter being very useful in obtaining certain overlapping peptides. The total chain length is 627 residues. Carbohydrate side chains were not found. The sequence is discussed with respect to the gross physical properties of the subunit, to homologies with subunit e and the cleavage specifities of the enzymes employed.
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July 1990,
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May 1979,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
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Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
W Schartau, and
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October 1979,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
W Schartau, and
F Eyerle, and
P Reisinger, and
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B Linzen
August 1980,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
W Schartau, and
F Eyerle, and
P Reisinger, and
H Geisert, and
H Storz, and
B Linzen
November 1980,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
W Schartau, and
F Eyerle, and
P Reisinger, and
H Geisert, and
H Storz, and
B Linzen
July 1990,
Proceedings of the National Academy of Sciences of the United States of America,
W Schartau, and
F Eyerle, and
P Reisinger, and
H Geisert, and
H Storz, and
B Linzen
September 1977,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
