Detail of "7339-87-9"

Reference

Conversion of (

Conversion of (.+-.)-synephrine into p-hydroxyphenylacetaldehyde by Arthrobacter synephrinum. A novel enzymic reaction.In this study， 7339-87-9 and 94-07-5 are also used. Veeraswamy, M,.; Devi, N. Abitha; Kutty, R. Krishnan; Rao, P. V. Subba (Dep. Biochem., Indian Inst. Sci., Bangalore, India). Biochem. J., 159(3), 807-9 (English) 1976. CODEN: BIJOAK. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Section cross-reference(s): 10 A partially purified enzyme from A. synephrinum catalyzed the conversion of (.+-.)-synephrine into p-hydroxyphenylacetaldehyde and methylamine. The enzyme, which had a pH optimum .apprx.8.0 and an abs. requirement for divalent cations such as Mg2+, was highly specific for synephrine, and was distinctly different from monoamine oxidase. .

Radioiodination of proteins by reductive alkylation

Radioiodination of proteins by reductive alkylation. Panuska, James R.; Parker, Charles W. (Sch. 7339-87-9 and 74-79-3 are also occured in this study. Med., Washington Univ., St. Louis, MO 63110, USA). Anal. Biochem., 160(1), 192-201 (English) 1987. CODEN: ANBCA2. ISSN: 0003-2697. DOCUMENT TYPE: Journal CA Section: 9 (Biochemical Methods) The use of the aliph. aldehyde, p-hydroxyphenylacetaldehyde as the reactive moiety in the radioiodination of proteins by reductive alkylation is described. The p-hydroxyphenyl group was radiolabeled with 125I and the compd. reacted through its aliph. aldehyde group with primary amino groups on proteins to form a reversible Schiff base linkage which could be stabilized with the mild reducing agent NaCNBH3. The introduction of the methylene group between the benzene ring and the aldehyde group increases its reactivity with protein amino groups permitting efficient labeling at low aldehyde concns. Radioiodinated proteins with high specific activity could be produced. The reductive alkylation procedure is advantageous in that the labeling conditions are mild, the reaction is specific for lysyl residues, and the modification of the e-ammonium group of lysine results in ionizable secondary amino groups, avoiding major changes in protein charge. .