Identification and characterization of barley mutants lacking glycine decarboxylase and carboxyl esterase activities

Conference · Tue May 01 00:00:00 EDT 1990 · Plant Physiology, Supplement; (USA)

OSTI ID:5851125

Blackwell, R; Lewis, K; Lea, P ^[1]

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1. Univ. of Lancaster (England)

A barley mutant has been isolated, from a selection of fifty air-sensitive seed-lines, using a standard gel stain technique which lacks carboxyl esterase activity, but has normal levels of carbonic anhydrase. In addition, two barley mutants lacking the ability to convert glycine to serine in the mitochondria, have been characterized. Both plants accumulate glycine in air and are unable to metabolize ({sup 14}C)glycine in the short-term. When ({sup 14}C)glycine was supplied over 2h LaPr 85/55 metabolized 90%, whereas the second mutant (LaPr 87/30) metabolized 10%. Results indicate that the mutation in LaPr 85/55 is almost certainly in the glycine transporter into the mitochondrion. The mutation in LaPr 87/30 has been shown, using western blotting, to be in both the P and H proteins, two of four proteins which comprise glycine decarboxylase (P, H, T and L).

• OSTI ID: 5851125
• Report Number(s): CONF-9007196-; CODEN: PPYSA
• Journal Information: Plant Physiology, Supplement; (USA), Vol. 93:1; Conference: Annual meeting of the American Society of Plant Physiologists, Indianapolis, IN (USA), 29 Jul - 2 Aug 1990; ISSN 0079-2241
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
ENZYMES
BIOCHEMICAL REACTION KINETICS
ANHYDRIDES
BARLEY
CARBON 14 COMPOUNDS
DECARBOXYLASES
LYASES
TRACER TECHNIQUES
CARBON-CARBON LYASES
CARBOXY-LYASES
CEREALS
GRAMINEAE
ISOTOPE APPLICATIONS
KINETICS
LABELLED COMPOUNDS
LILIOPSIDA
MAGNOLIOPHYTA
PLANTS
REACTION KINETICS
550201* - Biochemistry- Tracer Techniques