Evidence that Envelope and Thylakoid Membranes from Pea Chloroplasts Lack Glycoproteins.
نویسندگان
چکیده
Envelope and thylakoid membranes from pea (Pisum sativum var. Laxton's Progress No. 9) chloroplasts were analyzed for the presence of glycoproteins using two different approaches. First, the sugar composition of delipidated membrane polypeptides was measured directly using gas chromatographic analysis. The virtual absence of sugars suggests that plastid membranes lack glycoproteins. Second, membrane polypeptides separated by sodium dodecyl sulfate gel electrophoresis were tested for reactivity toward three different lectins: Concanavalin A, Ricinus communis agglutinin, and wheat germ agglutinin. In each case, there was no reactivity between any of the lectins and the plastid polypeptides. Microsomal membranes from pea tissues were used as a positive control. Glycoproteins were readily detectable in microsomal membranes using either of the two techniques. From these results it was concluded that pea chloroplast membranes do not contain glycosylated polypeptides.
منابع مشابه
Analysis of suborganellar fractions from spinach and pea chloroplasts for calmodulin-binding proteins
Purified chloroplasts from spinach and pea leaves were subfractionated into envelope, thylakoid, and stroma fractions and were analyzed for calmodulin-binding proteins using a 125I-calmodulin gel overlay assay. Calmodulin binding was primarily associated with a major polypeptide (Mr 33,000) in the envelope membrane fraction. In contrast, major calmodulin-binding proteins were not detected in th...
متن کاملAssembly of Newly Imported Oxygen-Evolving Complex Subunits in Isolated Chloroplasts: Sites of Assembly and Mechanism of Binding.
We have examined the assembly of the nuclear-encoded subunits of the oxygen-evolving complex (OEC) after their import into isolated intact chloroplasts. We showed that all three subunits examined (OE33, OE23, and OE17) partition between the thylakoid lumen and a site on the inner surface of the thylakoid membrane after import in a homologous system (e.g., pea or spinach subunits into pea or spi...
متن کاملCopper transport across pea thylakoid membranes.
The initial rate of Cu2+ movement across the thylakoid membrane of pea (Pisum sativum) chloroplasts was directly measured by stopped-flow spectrofluorometry using membranes loaded with the Cu(2+)-sensitive fluorophore Phen Green SK. Cu2+ transport was rapid, reaching completion within 0.5 s. The initial rate of uptake was dependent upon Cu2+ concentration and saturated at about 0.6 microm total...
متن کاملCOMMENTARY Import of proteins into chloroplasts
Chloroplasts are the sites of photosynthesis in eukaryotic plants and are able to harvest solar energy for the synthesis of carbon skeletons. They, like mitochondria, are enclosed by two membranes; the outer and the inner envelope. The latter is the actual permeability barrier between the cytosol and the chloroplast stroma and the site of different metabolite translocators that coordinate the m...
متن کاملOligomycin effects on ATPase and photophosphorylation of pea chloroplast thylakoid membranes.
Oligomycin inhibited the membrane-bound, Ca(2+)-dependent ATPase of pea (Pisum sativum var. Progress No. 9) chloroplasts up to 50%, but only after treating the membranes with trypsin, whether or not the trypsin step was needed for full activity. The energy-linked Mg(2+)-dependent (light- and dithiothreitol (DTT)-activated) ATPase of pea thylakoids could be inhibited up to 100% under specified c...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Plant physiology
دوره 70 1 شماره
صفحات -
تاریخ انتشار 1982