Spectrophotometric Determination of Acetylenic Compounds as Mercuric Acetate Complexes.

Siggia, Sidney.; Stahl, C. R.

doi:10.1021/ac60204a060

Cited by 7 publications

(1 citation statement)

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“…Protein was measured by the biuret method (Gornall et al, 1949). Glyoxal and glycolaldehyde were determined by the carbonyl assay (Bóhme and Winkler, 1954) at 510 and 590 nm (Wells, 1966), respectively, and 3-dimethylamino-1 -propyne was determined by the mercuric acetate method (Siggia and Stahl, 1963).…”

Section: Methodsmentioning

confidence: 99%

The structure of the covalent adduct formed by the interaction of 3-dimethylamino-1-propyne and the flavine of mitochondrial amine oxidase

Maycock¹,

Abeles²,

Salach³

et al. 1976

Biochemistry

124

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3-Dimethylamino-1-propyne irreversibly inactivates mitochondrial monoamine oxidase from bovine liver. The inactivation results in the loss of absorption in the 450-500-nm region of the flavine spectrum and a concomitant increase in absorbance at 410 nm. For the enzyme-bound adduct epsilon410 = 28000. The spectral properties of the adduct of the liver enzyme with 3-dimethylamino-1-propyne are similar to those observed when the pig kidney enzyme is inactivated with pargyline (Chuang et al. (1974), J. Biol. Chem. 249, 2381). From a proteolytic digest of the enzyme inactivated with labeled inhibitor a flavine peptide has been isolated which contains 1 mol of inactivator/mol of flavine. The chemical and spectral properties of the adduct are those of compounds containing the structure --N--CH==CH--CH==N+ less than. It was concluded that the flavine-inhibtor adduct is a N-5 substituted dihydroflavine and its structure has been determined.

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Section: Methodsmentioning

confidence: 99%