Dinitrosyl Iron Complexes and other Physiological Metabolites of Nitric Oxide: Multifarious Role in Plants.

This review considers dinitrosyl iron complexes (DNICs) and some other metabolites of nitric oxide (NO) in plants. Nitric oxide is vital for all living organisms, although its role in plants has been studied insufficiently compared with that in animals. We presume that the spectrum of its functions in plants is even wider than in animals.

[Physicochemical properties of proteins from wheat grown under high-contrast climatic conditions].

Studies using electrophoresis, gel chromatography, viscometry, and calorimetry revealed an interrelation of several physicochemical properties of proteins of soft wheat grown under conditions of cool and wet weather with rheological characteristics of gluten and dough and bread quality. The ratio of gliadin and albumin-globulin polypeptides in flour with short-tearing gluten was much lower compared to that in flour with normal gluten. Proteins from flour with short-tearing gluten, including the water-soluble and salt-soluble fraction, had a loose spatial structure.

[Physicochemical properties and specific structural features of protein-lipid composites of increased nutritive value].

Fractional and component compositions of protein-lipid composites with increased nutritive value (compared to the protein preparations from which they were produced) were studied based on solubility and electrophoretic behavior. Differences in the fractional compositions of proteins and the amounts of hydrogen, ionic, and hydrophobic bonds were found. It was demonstrated that the water-, salt-, and alkali-soluble fractions of proteins changed during the manufacturing of the composites with soybean and wheat bran flour; the water- and alkali-soluble fractions, with protein concentrate from bran.

[Ribosomal proteins of pea seeds behaving like anions at pH 8.6].

A group of proteins migrating to the anode at pH 8.6 under polyacrylamide gel electrophoresis was revealed in the total protein of non-dissociated KCl-washed pea seed ribosomes. No proteins with an isoelectric point below pH 4.

[Molecular weight hetergeneity of proteins of the ribosomes and ribosomal subunits from dry pea seeds].

The molecular weight distribution of the total protein of ribosomes and ribosomal subunits isolated from dry pea seeds was studied by electrophoresis in polyacrylamide gel, containing sodium dodecyl sulfate. It was demonstrated that overall protein of 80 S ribosomes is separated into a number of fractions with molecular weights of 10000-64000. Treatment of ribosomes with 0.