Purification of adhesive proteins from mussels.
The adhesive polyphenolic proteins from the mussels Mytilus chilensis and Choromytilus chorus have been purified based on their solubility in dilute perchloric acid and on differential precipitation with acetone containing about 0.3 N HCl. The specific activity of the proteins obtained was 0.16 mg of 3,4-dihydroxyphenylalanine per milligram of protein, or higher. The proteins have an apparent molecular weight of about 100,000 and they contain a high proportion of 3,4-dihydroxyphenylalanine, lysine, and proline.
Pardo
J
J
Instituto de Bioquímica, Facultad de Ciencias, Universidad Austral de Chile, Valdivia.
Gutierrez
E
E
Sáez
C
C
Brito
M
M
Burzio
L O
LO
D000096:Acetone; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D049872:Bivalvia / Q000737:chemistry*; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000302:isolation & purification*; D011232:Chemical Precipitation; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D010472:Perchlorates; D012995:Solubility
D000596:Amino Acids; D015815:Cell Adhesion Molecules; D010472:Perchlorates; D000096:Acetone