Carbohydrate moieties of molluscan Rapana venosa hemocyanin.
Using Zn2+ ions as new method, several FUs have been isolated from molluscan Hc Rapana venosa without formation of non-functional proteolytic side products. N-terminal sequences of these fragments in comparison with FUS from other gastropodan Hcs show a very high degree of structural identity. Four Fus, purified from enzyme-treated structural subunits RvH1 and RvH2 (RvH1-a, RvH1-f, RvH2-a and RvH2-e) show identical N-terminal sequences compared to fragments isolated after treatment with Zn2+ ions. However, in some cases trypsin cleaves RvH chains at different positions if compared to the Zn2+ treatment. To analyze the oligosaccharide composition of two FUS from the first structural subunit of Rapana Hc, RvH1-a and RvH1-f, several techniques were applied: capillary electrophoresis, MALDI-MS, ESI-MS in combination with glycosidase digestions. On basis of these results and the determined amino acid sequence two N-linkage sites were identified in the FU RvH1-a, but only one in the FU RvH1-f.
Dolashka-Angelova
Pavlina
P
Institute of Organic Chemistry, Bulgarian Academy of Sciences, Sofia, Bulgaria. pda54@yahoo.com
Beck
A
A
Dolashki
A
A
Stevanovic
S
S
Beltramini
M
M
Salvato
B
B
Hristova
R
R
Velkova
L
L
Voelter
W
W
D000595:Amino Acid Sequence; D000818:Animals; D002241:Carbohydrates / Q000737:chemistry*; D006433:Hemocyanins / Q000737:chemistry*; D008969:Molecular Sequence Data; D008974:Mollusca / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D002241:Carbohydrates; D006433:Hemocyanins