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Subcellular immuno‐localization, amino acid composition and partial amino acid sequences of α‐l,4‐glucan phosphorylase of Gracilaria spp (Rhodophyta)
Author(s) -
Yu S.,
GómezPinchetti J.L.,
GarciaReina G.,
Ek B.,
Pedersén M.
Publication year - 1993
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1993.tb01780.x
Subject(s) - glycogen phosphorylase , biochemistry , amino acid , biology , enzyme , glucan , cytosol , cell wall , chloroplast , gene
Antibodies have been raised against an α‐l,4‐glucan phosphorylase (EC 2. 4. 1. 1) purified from the red alga Gracilaria chilensis. Localization of α‐l,4‐glucan phosphorylase in thin sections of G. chilensis and G. tenuistipitata was performed using immuno‐gold labelling and transmission electron microscopy. The enzyme was localized in the cytosol and around the cytosolic starch granules of the algal cells. The labelling was not associated with the chloroplast or the cell wall. Amino acid composition of the red algal phosphorylase was quite similar to that of potato tuber and rabbit muscle phosphorylases. Partial amino acid sequences showed 48, 54 and 65% homology with the rabbit, potato and Escherichia coli enzymes, respectively.