ISSN:
1399-3054
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
α-1,4-Glucan phosphorylase (EC 2.4.1.1) from the red seaweed Gracilaria sordida(Harv.) W. Nelson was adsorbed onto starch-Sepharose 6B and Sephacryl S-300 under specified conditions. The algal enzyme was purified to homogeneity by these two steps. A molecular weight of 97.4 kDa was observed on SDS-polyacrylamide gel electrophoresis under reducing conditions, while the native molecular weight was 240 kDa asrevealed by 8-25% native gradient gel electrophoresis or 245 kDa by gel filtration. The pI of the enzyme was 5.4. It had a Km of 227, 264, 285, and 453 μg ml-1, respectively, towards glycogen, amylopectin, amylose, and maltodextrin. The enzyme activity was inhibited by cyclohexaamylose, ADP-glucose, and UDP-glucose. In contrast to other plant sources, cell-free extracts of G. sordida contained only one form of phosphorylase.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1399-3054.1991.tb02122.x
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