Reference

Sodium cyanoborohydride in the immobilization of proteins to glutaraldehyde-activated aminoalkyl silica

Sodium cyanoborohydride in the immobilization of proteins to glutaraldehyde-activated aminoalkyl silica.Some chemicals with cas registry numbers like 25895-60-7 and 9025-70-1 are also used. Miller, Arthur W.; Robyt, John F. (Dep. Biochem. Biophys., Iowa State Univ., Ames, IA 50011, USA). Biotechnol. Bioeng., 25(11), 2795-800 (English) 1983. CODEN: BIBIAU. ISSN: 0006-3592. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Section cross-reference(s): 9 The effects of NaBH3CN on protein immobilization on glutaraldehyde-activated aminoalkyl silica were examd. at high-protein loading (bovine serum albumin, 20 mg/mL silica) and at low-protein loading (dextranase, 0.1 mg/mL silica). NaBH3CN stabilized the displacement of immobilized dextranase by dextran when present during the immobilization procedure. The magnitude of this effect decreased with the length of immobilization; with a 2-h immobilization, NaBH3CN caused 42-59% more activity to be irreversibly immobilized, whereas after a 24-h immobilization, an improvement of only 13-19% was effected. With a 24-h immobilization, NaBH3CN decreased the amt. of albumin immobilized, but increased the quantity of protein immobilized after only a 2-h immobilization. NaBH3CN acts by reducing the time for formation of stable linkages (redn. of the Schiff bases) between the protein and the carrier; it does not increase the no. of potential immobilization sites. .

Characterization of antiserums to the addition product formed by the nonenzymic reaction of 16a-hydroxyestrone with albumin

Characterization of antiserums to the addition product formed by the nonenzymic reaction of 16a-hydroxyestrone with albumin. Bucala, Richard; Cerami, Anthony (Lab. Med. Biochem., Rockefeller Univ., New York, NY 10021, USA). Mol. Immunol., 20(12), 1289-92 (English) 1983. CODEN: MOIMD5. ISSN: 0161-5890. DOCUMENT TYPE: Journal CA Section: 15 (Immunochemistry) Section cross-reference(s): 2 16a-Hydroxyestrone (16aOHE) has been shown previously to react nonenzymically with proteins via a Heyns rearrangement of a Schiff base intermediate. Albumin modified by the addn. of 16aOHE is immunogenic, despite a relatively low molar substitution. High-titer antisera can be elicited which have a very high affinity toward the estrogen hapten. Cross-reactivity anal. 25895-60-7 and 566-76-7 are also in the experiment. reveals a high specificity for the phenolic A-ring and a lack of specificity to chem. substituents in the D-ring, the site of covalent linkage. The antiserum reacts equally well with 16aOHE-peptides or with 16aOHE-lysine, suggesting the utility of this antiserum in analyzing either enzymically or chem. hydrolyzed proteins for the presence of 16aOHE adducts. Immunochem. anal. of proteins modified by 16aOHE may provide insight into the pathogenesis of systemic lupus erythematosus, an autoimmune disease in which elevated levels of 16aOHE occur. .