The molecular weight of beta-1,3-glucanase from the marine mollusc Spi
sula sachalinensis has been determined using liquid chromatography, el
ectrophoresis, and sedimentation analysis. The methods employed for es
tablishing the molecular weight of native enzyme, gel filtration on va
rious matrices and ultracentrifugation in buffer systems, gave the mol
ecular weight value of 22 kD. However, under denaturing conditions (ge
l filtration in 6 M guanidine chloride, high performance exclusion chr
omatography in trifluoroacetic acid, sodium dodecyl sulfate gel electr
ophoresis) the molecular weight value was around 38 +/- 1 kD. Such a l
owering of the molecular weight value for S. sachalinensis beta-1,3-gl
ucanase which was observed also for other beta-1,3-glucanases suggests
that the enzyme has a compact conformation and its movement during ge
l filtration is slowed down in comparison with standard proteins.