Multiple invertebrate lysozymes in blue mussel (Mytilus edulis).
Initial analyses of lysozyme activities in individual blue mussels Mytilus edulis indicated variations in features of activity from the crystalline style to the remaining body parts (the soft body). Two separate larger scale lysozyme isolations were performed employing extracts from 1000 styles and 50 soft bodies, respectively. The soft body origin contained one, or one major, lysozyme that was purified to homogeneity. This 13 kDa protein, designated bm-lysozyme, was sequence-analysed and found to represent the product of a recently published invertebrate-type lysozyme gene from M. edulis. Three additional lysozymes were isolated from the style extract and one of them was fully purified. All four lysozymes showed different profiles of enzymatic features such as responses to pH, ionic strengths and divalent cations. From the results and the profound differences demonstrated we believe that the observed multiple forms of lysozyme activities in blue mussel reflect multiple genes instead of individual lysozyme variants and that the lysozymes serve different functions in the blue mussel.
Olsen
Ørjan M
ØM
Marine Biotechnology and Fish Health, Norwegian Institute of Fisheries and Aquaculture, P.O. Box 6122, Tromsø N-9291, Norway.
Nilsen
Inge Waller
IW
Sletten
Knut
K
Myrnes
Bjørnar
B
D000595:Amino Acid Sequence; D000818:Animals; D049872:Bivalvia / Q000201:enzymology*; D002412:Cations; D006863:Hydrogen-Ion Concentration; D007448:Invertebrates / Q000201:enzymology; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D009994:Osmolar Concentration; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein
D002412:Cations; D009113:Muramidase