GENSTUDIEN AN PISUM SATIVUM VI-VIII

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...

The isoperoxidases of Pisum sativum.

The heterogeneity of the peroxidases in peas was examined by starch gel electrophoresis. Comparisons were made between tall and dwarf cultivars and among organ systems developed in light and darkness. Isoperoxidase bands could be grouped as cathodic, anodic and near-neutral (at pH 9.0) types. The cathodic set stained well with guaiacol oxidation products whereas some anodic bands reacted prefer...

Properties of an Aminotransferase of Pea (Pisum sativum L.).

A transaminase (aminotransferase, EC 2.6.1) fraction was partially purified from shoot tips of pea (Pisum sativum L. cv. Alaska) seedlings. With alpha-ketoglutarate as co-substrate, the enzyme transaminated the following aromatic amino acids: d,l-tryptophan, d,l-tyrosine, and d,l-phenylalanine, as well as the following aliphatic amino acids: d,l-alanine, d,l-methionine, and d,l-leucine. Of othe...

Concerning artificial crossing in Pisum sativum.

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...