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Phosphoglucomutase activity in aspergillus niger

✍ Scribed by Khanna, Rajni ;Tewari, K. K.

Publisher
Springer-Verlag
Year
1963
Weight
511 KB
Volume
45
Category
Article
ISSN
0003-9276

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✦ Synopsis

Phosphoglucomutase, the enzyme which catalyses the intcrconversion of glucose-l-phosphate and glucose-6-phosphate, was crystallized from r a b b i t skeletal muscle b y β€’AJJAIr (1948) and b y JAGANNATHAN and LUCK (1949) and obtained in a highly purified form from yeast b y ~. AJJAI~ and McCoY (1958). The kinetics of the reaction have been extensively studied b y several groups of workers, one of the most comprehensive studies being t h a t of MILST~I~ (1961, a,b,e). The enzyme is characterized b y a complex requirement for cofactors. There are scanty reports on this enzyme from plant tissues (vide SISAI~YA~ and KOBYAKOVA 1949). The enzyme does not seem to have been studied in sufficient detail in molds.

As a preliminary to characterizing the enzyme in Aspergillus niger, the present authors u n d e r t o o k a s t u d y of the phosphoglucomutase a c t i v i t y in homogenates of the mycelium of AspergiUus niger. A point of special interest was the elucidation whether the hexokinase inhibitor in spores of Asp. niger (NA~TDAN, TEWAIr and KI~ISHNAN 1962) would have a n y influence on phosphoglueomutase. The results obtained are reported in this paper.

Materials and methods

1. Culture o/organism

Strain NRI~L 599 of Asp. niger was cultured stationary in synthetic basal and

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