Protein damage and degradation by oxygen radicals. I. general aspects.

Glutaraldehyde possesses unique characteristics that render it one of the most effective protein crosslinking reagents. It can be present in at least 13 different forms depending on solution conditions such as pH, concentration, temperature, etc. Substantial literature is found concerning the use of glutaraldehyde for protein immobilization, yet there is no agreement about the main reactive species that participates in the crosslinking process because monomeric and polymeric forms are in equilibrium. Glutaraldehyde may react with proteins by several means such as aldol condensation or Michael-type addition, and we show here 8 different reactions for various aqueous forms of this reagent. As a result of these discrepancies and the unique characteristics of each enzyme, crosslinking procedures using glutaraldehyde are largely developed through empirical observation. The choice of the enzyme-glutaraldehyde ratio, as well as their final concentration, is critical because insolubilization of the enzyme must result in minimal distortion of its structure in order to retain catalytic activity. The purpose of this paper is to give an overview of glutaraldehyde as a crosslinking reagent by describing its structure and chemical properties in aqueous solution in an attempt to explain its high reactivity toward proteins, particularly as applied to the production of insoluble enzymes.

https://www.future-science.com/doi/pdf/10.2144/04375RV01

Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking.

Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins

/pdf/the-structure-biosynthesis-and-function-of-glycosylated-4rbegebbn2.pdf

The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes.

Chemical modification of proteins is an important tool for probing natural systems, creating therapeutic conjugates and generating novel protein constructs. Site-selective reactions require exquisite control over both chemo- and regioselectivity, under ambient, aqueous conditions. There are now various methods for achieving selective modification of both natural and unnatural amino acids--each with merits and limitations--providing a 'toolkit' that until 20 years ago was largely limited to reactions at nucleophilic cysteine and lysine residues. If applied in a biologically benign manner, this chemistry could form the basis of true Synthetic Biology.

/pdf/selective-chemical-protein-modification-4z476j40wm.pdf

Selective chemical protein modification

Labeling of proteins by reductive methylation using sodium cyanoborohydride.

Phosphonoglycan. A major polysaccharide constituent of the amoeba plasma membrane contains 2-aminoethylphosphonic acid and 1-hydroxy-2-aminoethylphosphonic acid.

Lipophosphonoglycan of the Plasma Membrane of Acanthamoeba castellanii: ISOLATION FROM WHOLE AMOEBAE AND IDENTIFICATION OF THE WATER-SOLUBLE PRODUCTS OF ACID HYDROLYSIS

Dorr Gellatly Dearborn

Papers

Labeling of proteins by reductive methylation using sodium cyanoborohydride.

Phosphonoglycan. A major polysaccharide constituent of the amoeba plasma membrane contains 2-aminoethylphosphonic acid and 1-hydroxy-2-aminoethylphosphonic acid.

Lipophosphonoglycan of the Plasma Membrane of Acanthamoeba castellanii: ISOLATION FROM WHOLE AMOEBAE AND IDENTIFICATION OF THE WATER-SOLUBLE PRODUCTS OF ACID HYDROLYSIS

Lipophosphonoglycan of the plasma membrane of A canthamoeba castellanii. Inositol and phytosphingosine content and general structural features.

Lipophosphonoglycan of the Plasma Membrane of Acanthamoeba castellanii FATTY ACID COMPOSITION