Premium
Purification and molecular properties of acid phosphatase from sycamore cell walls
Author(s) -
CRASNIER MARTINE,
NOAT GEORGES,
RICARD JACQUES
Publication year - 1980
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/1365-3040.ep11581714
Subject(s) - acid phosphatase , homogeneous , biochemistry , polyacrylamide gel electrophoresis , enzyme , glycoprotein , protease , chemistry , gel electrophoresis , electrophoresis , amino acid , biology , microbiology and biotechnology , physics , thermodynamics
. An acid phosphatase is isolated and purified to homogeneity from sycamore cell walls. The enzyme, which has a molecular weight close to 100,000, is a glycoprotein and is most probably made up of one polypeptide chain only. Its amino acid composition has been determined. Although homogeneous to polyacrylamide gel electrophoresis under non‐denaturing conditions, the enzyme preparation still contains protease traces that tend to split polypeptide chain in two fragments.