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., Upton, NY
- OSTI ID:
- 7218593
- Journal Information:
- Plant Physiol.; (United States), Journal Name: Plant Physiol.; (United States) Vol. 59:6; ISSN PLPHA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
ACID PHOSPHATASE
BIOCHEMICAL REACTION KINETICS
BIOLOGICAL LOCALIZATION
BIOMASS
CARBOHYDRATES
CARBOXYPEPTIDASE
CATALYSIS
CELL CONSTITUENTS
DNA-ASE
ENERGY SOURCES
ENZYMES
ESTERASES
FLOWERS
GALACTOSIDASE
GLYCOSIDES
GLYCOSYL HYDROLASES
HYDROLASES
KINETICS
LYSOSOMES
METABOLISM
ORGANIC COMPOUNDS
ORGANOIDS
PEPTIDE HYDROLASES
PH VALUE
PHOSPHATASES
PHOSPHOTRANSFERASES
PLANT CELLS
PLANT TISSUES
PLANTS
REACTION KINETICS
RENEWABLE ENERGY SOURCES
RNA-ASE
TRANSFERASES