Localization of acid hydrolases in protoplasts. Examination of the proposed lysosomal function of the mature vacuole
The development of techniques to isolate and purify relatively large quantities of intact vacuoles from mature tissues permits direct biochemical analysis of this ubiquitous mature plant cell organelle. Vacuoles and a fraction enriched in soluble cytoplasmic constituents were quantitatively prepared from Hippeastrum flower petal protoplasts. Vacuolar lysate and soluble cytoplasmic fractions were examined for acid hydrolase activities commonly associated with animal lysosomes, and pH optima were determined. Esterase, protease, carboxypeptidase, ..beta..-galactosidase, ..cap alpha..-glycosidase and ..beta..-glycosidase, not found in the vacuole lysate fraction, were components of the soluble cytoplasmic fraction. Acid phosphatase, RNase and DNase were present in both fractions. Vacuolar enzyme activities were also examined as a function of flower development from bud through senescent stages. The data obtained are not consistent with the concept that the mature plant cell vacuole functions as a generalized lysosome.
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- OSTI ID:
- 7218593
- Journal Information:
- Plant Physiol.; (United States), Vol. 59:6
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
HYDROLASES
BIOLOGICAL LOCALIZATION
PLANT CELLS
ACID PHOSPHATASE
BIOCHEMICAL REACTION KINETICS
CARBOXYPEPTIDASE
CATALYSIS
CELL CONSTITUENTS
DNA-ASE
ENZYMES
ESTERASES
FLOWERS
GALACTOSIDASE
GLYCOSIDES
LYSOSOMES
METABOLISM
ORGANOIDS
PH VALUE
PLANT TISSUES
PLANTS
RNA-ASE
BIOMASS
CARBOHYDRATES
ENERGY SOURCES
GLYCOSYL HYDROLASES
KINETICS
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PHOSPHATASES
PHOSPHOTRANSFERASES
REACTION KINETICS
RENEWABLE ENERGY SOURCES
TRANSFERASES
550200* - Biochemistry