1Nuclear Research Laboratory, IARI, New Delhi 110012, India
Division of Biochemistry, Indian Agricultural Research Institute, New Delhi 110012, India
* Corresponding author. E-mail basu@iari.ernet.in
Starch phosphorylase (α-1,4 glucan: orthophosphate α-D-glucosyl transferase, EC 2.4.1.1) was partially purified from triticale by ammonium sulphate fractionation and chromatography on Sephadex G-200. Three active fractions were obtained, which differed in their kinetic properties and activities in the presence of certain glycoiytic and Krebs cycle intermediates. These fractions may have specific functions in starch synthesis during grain development. The isoenzymic fraction Ell, in particular, may have a regulatory function by controlling formation of primers from oligosaccharides.
starch phosphorylase, isoenzymes, triticale, shrivelling, oligosaccharide primers, maltose, maltotriose
