DNA methylase from Pisum sativum

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DNA methylase from Pisum sativum.

DNA methylase activity was detected in nuclei from pea shoots. The enzyme can only be extracted by low-salt treatment if the nuclei are pretreated with micrococcal nuclease. Only a single enzyme was detected, and it was purified to a specific activity of 1620 units/mg of protein. It has an Mr of 160,000 on gel filtration and SDS/PAGE. Pea DNA methylase methylates cytosine in all four dinucleoti...

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Ribosomal DNA Amounts in PISUM SATIVUM.

Different varieties of peas have different proportions of rDNA in their genomes; there is no obvious correlation between the proportions and seed or leaf size. The rDNA proportions in root tips, seedlings, leaves and in the cotyledon cells of high DNA content, were compared in four varieties. In three, there was no difference between tissues; the fourth showed an amplification of rRNA genes in ...

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Anti -Hcv Lectin from Egyptian Pisum sativum

Lectins are carbohydrate binding proteins expressed in plants, animals and microorganisms and have been used to probe the surface properties of a wide range of prokaryotic and eukaryotic cells. The implication of some lectin molecules in several physiological processes has been claimed. The aim of this work is to purify the lectin from Egyptian pea (Pisum sativum) seeds and study its biochemica...

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Polyadenylate-Binding Protein from Pea (Pisum sativum)'

A polyadenylate-binding protein (PABP) was purified from cellfree extracts prepared from pea seedlings (Pisum sativum) by ammonium sulfate precipitation and Affi-Gel Blue and polyadenylate-Sepharose 4B affinity chromatography. The final preparation from polyadenylate-Sepharose 4B columns contained a single 70-kilodalton polypeptide with high polyadenylate-binding activity. The purified protein ...

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DNA Strand-Transfer Activity in Pea (Pisum sativum L.) Chloroplasts.

The occurrence of DNA recombination in plastids of higher plants is well documented. However, little is known at the enzymic level. To begin dissecting the biochemical mechanism(s) involved we focused on a key step: strand transfer between homologous parental DNAs. We detected a RecA-like strand transfer activity in stromal extracts from pea (Pisum sativum L.) chloroplasts. Formation of joint m...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1991

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj2730469