Identification of UDPG-binding polypeptides and purified (1,3)-. beta. -glucan synthase by photoaffinity labelling with 5-azido-UDPG

Journal Article · Sat Apr 01 04:00:00 EST 1989 · Plant Physiology, Supplement; (USA)

OSTI ID:6650372

Frost, D J; Wu, A; Read, S M; Wasserman, B P ^[1]; Drake, R R; Haley, B E ^[2]

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1. Rutgers Univ., New Brunswick, NJ (USA)
2. Univ. of Kentucky, Lexington (USA)

The photoaffinity probe 5-azido-uridine 5{prime}-{beta}-({sup 32}P)-diphosphate glucose was used to identify the major UDPG-binding polypeptide of red beet (1,3)-{beta}-glucan synthase. Glucan synthase was purified from plasma membranes by sequential solubilization with CHAPS followed by product entrapment. Two major polypeptides at 72 and 54 kD were labelled by probe. Labelling of both was abolished with increasing levels of cold UDPG. However, labelling of the 54 kD polypeptide was dependent upon the presence of divalent cations. These data suggest that the 54 kD polypeptide is a substrate-binding and cation-regulated component of the glucan synthase complex.

• OSTI ID: 6650372
• Journal Information: Plant Physiology, Supplement; (USA), Journal Name: Plant Physiology, Supplement; (USA) Vol. 89:4; ISSN PPYSA; ISSN 0079-2241
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AFFINITY
ALDEHYDES
BEETS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CARBOHYDRATES
DAYS LIVING RADIOISOTOPES
ENZYMES
FOOD
GLUCOSE
HEXOSES
HYDROLASES
ISOTOPE APPLICATIONS
ISOTOPES
LABELLING
LIGHT NUCLEI
MAGNOLIOPHYTA
MAGNOLIOPSIDA
MONOSACCHARIDES
NUCLEI
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
PEPTIDES
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
PLANTS
POLYPEPTIDES
PROTEINS
RADIOISOTOPES
SACCHARIDES
TRACER TECHNIQUES
VEGETABLES