Direct electron transfer between copper-containing proteins and electrodes

The D-galactose oxidase of Polyporus circinatus.

Publisher Summary Carbohydrate oxidases are found in all kingdoms of life but are mostly found in fungi. Their natural role is not always clear. Usage of molecular oxygen as electron acceptor is not a logical choice when the enzyme is part of a catabolic pathway. This chapter provides an overview of the occurrence and properties of carbohydrate oxidases. The physiological role of the different enzymes is discussed in relation to their origin, and the catalytic and structural properties are discussed in relation to their family background. It also provides a summary of the biocatalytic applications of carbohydrate oxidases. Carbohydrate oxidases are valuable enzymes for several applications. They are relatively stable and do not need expensive coenzymes. Carbohydrate oxidases are widely used in diagnostic applications, in the food and drinks industry, and for carbohydrate synthesis. They are also used for bleaching (production of H2O2) and as oxygen scavenger.

Occurrence and biocatalytic potential of carbohydrate oxidases.

Enzymic methods for the micro assay of D-mannose, D-glucose, D-galactose, and L-fucose from acid hydrolyzates of glycoproteins

Protein glycosylation involves the co-translational or post-translational addition of glycans to proteins and is a crucial protein modification in health and disease. The aim of glycoproteomics is to understand how glycosylation shapes biological processes by understanding peptide sequences, glycan structures and sites of modification in a system-wide context. Over the past two decades, mass spectrometry (MS) has emerged as the primary technique for studying glycoproteins, with intact glycopeptide analysis — the study of glycopeptides decorated with their native glycan structures — now a preferred approach across the community. In this Primer, we discuss glycoproteomic methods for studying glycosylation classes, including best practices and critical considerations. We summarize how glycoproteomics is used to understand glycosylation at a systems level, with a specific focus on N-linked and O-linked glycosylation (both mucin-type and O-GlcNAcylation). We cover topics that include sample selection; techniques for protein isolation, proteolytic digestion, glycopeptide enrichment and MS fragmentation; bioinformatic platforms and applications of glycoproteomics. Finally, we give a perspective on where the field is heading. Overall, this Primer outlines the current technologies, persistent challenges and recent advances in the exciting field of glycoproteomics. 

Glycoproteomics

The effect of certain phenothiazines on the structure and metabolic activity of sarcosomes of guinea pig heart.

THE inhibitory effect of thyroxine on oxidative phosphorylation of mammalian mitochondria was demonstrated by Lardy and Feldott1, and Maley and Lardy2.

Reversal by Acetylcholine of the Inhibition by Thyroxine of Oxidative Phosphorylation in Guinea-pig Heart Sarcosomes

Inhibition by Phenothiazinic Compounds of the Effect Of 2,4-Dinitrophenol on the Respiration of Heart Muscle Sarcosomes

Inhibition by phenothiazinic compounds of the effect of 2,4-dinitrophenol on the respiration of heart muscle sarcosomes.

Galactose Oxidase from Polyporus circinatus, Fr

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The effect of certain phenothiazines on the structure and metabolic activity of sarcosomes of guinea pig heart.

Reversal by Acetylcholine of the Inhibition by Thyroxine of Oxidative Phosphorylation in Guinea-pig Heart Sarcosomes

Inhibition by phenothiazinic compounds of the effect of 2,4-dinitrophenol on the respiration of heart muscle sarcosomes.

Galactose Oxidase from Polyporus circinatus, Fr