Integration of Ultrasound into the Development of Plant-Based Protein Hydrolysate and Its Bio-Stimulatory Effect for Growth of Wheat Grain Seedlings In Vivo.

This study was dedicated to increasing the efficiency of producing plant-based protein hydrolysate using traditional and non-traditional treatments. Low- and high frequency ultrasound (US) at different intensities were applied to corn steep liquor (CSL) at 50 °C for 30 min, and enzymatic hydrolysis was performed using industrially produced alkaline protease. The efficiency of US and enzymatic treatments was characterized by protein solubility (soluble protein (SP) content, hydrolyzed protein (HP) concentration, and free amino acid (FAA) profile) and kinetic parameters: Michaelis-Menten constant (KM) and apparent breakdown rate constant (kA).

Nuclear proteome of virus-infected and healthy potato leaves.

Background: Infection of plants by viruses interferes with expression and subcellular localization of plant proteins. Potyviruses comprise the largest and most economically damaging group of plant-infecting RNA viruses. In virus-infected cells, at least two potyviral proteins localize to nucleus but reasons remain partly unknown.

Differential Requirement of the Ribosomal Protein S6 and Ribosomal Protein S6 Kinase for Plant-Virus Accumulation and Interaction of S6 Kinase with Potyviral VPg.

Ribosomal protein S6 (RPS6) is an indispensable plant protein regulated, in part, by ribosomal protein S6 kinase (S6K) which, in turn, is a key regulator of plant responses to stresses and developmental cues. Increased expression of RPS6 was detected in Nicotiana benthamiana during infection by diverse plant viruses. Silencing of the RPS6 and S6K genes in N.

Application of multiplexed cysteine-labeled complex protein sample for 2D electrophoretic gel alignment.

The analysis of cellular subproteomes by 2DE is hampered by the difficulty of aligning gel images from samples that have very different protein composition. Here, we present a sensitive and cost-effective fluorescent labeling method for analyzing protein samples that is not dependent on their composition. The alignment is guided by inclusion of a complex mixture of proteins that is co-run with the sample.