A. Vanwormhoudt et al., AMYLASE POLYMORPHISM IN CRUSTACEA DECAPODA - ELECTROPHORETIC AND IMMUNOLOGICAL STUDIES, Biochemical systematics and ecology, 23(2), 1995, pp. 139-149
Alpha-amylase polymorphism was studied in 40 species of crustaceans be
longing to four infraorders of Decapoda. Specific activities of alpha-
amylases from hepatopancreas extracts of the same species were also me
asured. Very low specific activities were measured for Carcinus, Munid
a, Nephrops and Palinurus, whilst high activities were measured for sh
rimps and crabs. Amylases from one species of each of the four infraor
ders of Decapoda were purified by affinity chromatography. Very few di
fferences in the specific activities of the pure enzymes were detected
. The amylase content of crude extracts ranges between 0.1% of total p
rotein, from the hepatopancreas in Carcinus maenas and Eupagurus bernh
ardus, to 1% in Penaeus vannamei and Procambarus clarkii.The apparent
molecular weight, determined by denaturating electrophoresis, was 55 k
Da for Eupagurus and Procambarus amylases but only about 30 kDa for Ca
rcinus and Penaeus amylases. Using immunodiffusion, rocket immunoelect
rophoresis and enzyme inhibition with antibodies against Palaemon serr
atus alpha-amylase, we have shown that all the Decapod alpha-amylases
are immunologically related but that they are different from those of
Copepods, Bacillus or pig pancreatic amylases. The use of these data f
or phylogenetic analysis is discussed.