chlorophyll-a and 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate

chlorophyll-a has been researched along with 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate* in 1 studies

Other Studies

1 other study(ies) available for chlorophyll-a and 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate

Article	Year
Chloroplast biogenesis 84: solubilization and partial purification of membrane-bound [4-vinyl]chlorophyllide a reductase from etiolated barley leaves. Analytical biochemistry, 2001, Aug-15, Volume: 295, Issue:2 [4-Vinyl] chlorophyllide a reductase (4VCR) is a key enzyme of the chlorophyll (Chl) biosynthetic pathway. It catalyzes the conversion of divinyl chlorophyllide (Chlide) a to monovinyl Chlide a by reduction of the vinyl group at position 4 of the macrocycle to ethyl. 4VCR is a membrane-bound enzyme, embedded in etioplast and etiochloroplast membranes. A study of the regulation and properties of this enzyme is mandatory for a comprehensive understanding of the biosynthetic heterogeneity of Chl biosynthesis. Solubilization and partial purification of 4VCR are described for the first time. The enzyme was solubilized with 5 mM Chaps and was partially purified by chromatography on DEAE-Sephacel and Cibacron Blue 3GA-1000 agarose. An overall 20-fold purification was achieved. The partially purified enzyme was stable for several months at -80 degrees C. Topics: Cell Membrane; Chlorophyll; Cholic Acids; Chromatography; Dithiothreitol; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Glycerol; Hordeum; Light; Oxidoreductases; Plant Leaves; Solubility	2001

Article

Year

Chloroplast biogenesis 84: solubilization and partial purification of membrane-bound [4-vinyl]chlorophyllide a reductase from etiolated barley leaves.

Analytical biochemistry, 2001, Aug-15, Volume: 295, Issue:2

[4-Vinyl] chlorophyllide a reductase (4VCR) is a key enzyme of the chlorophyll (Chl) biosynthetic pathway. It catalyzes the conversion of divinyl chlorophyllide (Chlide) a to monovinyl Chlide a by reduction of the vinyl group at position 4 of the macrocycle to ethyl. 4VCR is a membrane-bound enzyme, embedded in etioplast and etiochloroplast membranes. A study of the regulation and properties of this enzyme is mandatory for a comprehensive understanding of the biosynthetic heterogeneity of Chl biosynthesis. Solubilization and partial purification of 4VCR are described for the first time. The enzyme was solubilized with 5 mM Chaps and was partially purified by chromatography on DEAE-Sephacel and Cibacron Blue 3GA-1000 agarose. An overall 20-fold purification was achieved. The partially purified enzyme was stable for several months at -80 degrees C.

Topics: Cell Membrane; Chlorophyll; Cholic Acids; Chromatography; Dithiothreitol; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Glycerol; Hordeum; Light; Oxidoreductases; Plant Leaves; Solubility

2001