Amino-acid sequence of the cooperative dimeric myoglobin from the radular muscles of the marine gastropod Nassa mutabilis.
The complete amino-acid sequence of the dimeric and cooperative myoglobin from the radular muscles of Nassa mutabilis, a common edible gastropod mollusc on the Italian coast, has been determined. The molecule is a homodimer. The monomer is composed of 147 amino-acid residues, with a molecular mass of 15,760 Da. Its sequence is homologous with those of the dimeric myoglobins of the gastropod molluscs of the Prosobranchia subclass Busycon canaliculatum (63% conserved residues) and Cerithidea rhizophorarum (46% conserved residues). The rate of autoxidation to met-myoglobin of N. mutabilis oxymyoglobin at 25 degrees C is strongly pH-dependent with relative minimal rate values in the pH range 7 to 8.
Parente
A
A
Dipartimento di Chimica Organica e Biologica, Università di Napoli, Italy.
Verde
C
C
Malorni
A
A
Montecucchi
P
P
Aniello
F
F
Geraci
G
G
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D006863:Hydrogen-Ion Concentration; D007558:Italy; D008969:Molecular Sequence Data; D008974:Mollusca / Q000737:chemistry*; D009132:Muscles / Q000737:chemistry; D009211:Myoglobin / Q000737:chemistry* / Q000302:isolation & purification; D014357:Trypsin
D000596:Amino Acids; D009211:Myoglobin; D002918:Chymotrypsin; D014357:Trypsin; D003488:Cyanogen Bromide