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Biochemistry, Biophysics, and Structural Biology Commons

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Chemistry Faculty Publications

Biochemistry

1966

Articles 1 - 4 of 4

Full-Text Articles in Biochemistry, Biophysics, and Structural Biology

Investigations On Lignins And Lignification Pt. Xxxi Characterization Of Metasequoia 'Milled-Wood' Lignin / By Michael J. Reale, Donald D. Clarke, Walter J. Schubert And F. F. Nord Laboratory Of Organic Chemistry And Enzymology), Fordham University, Bronx, New York, Michael J. Reale, Donald Dudley Clarke Phd, Walter J. Schubert, Friedrich F. Nord Jan 1966

Investigations On Lignins And Lignification Pt. Xxxi Characterization Of Metasequoia 'Milled-Wood' Lignin / By Michael J. Reale, Donald D. Clarke, Walter J. Schubert And F. F. Nord Laboratory Of Organic Chemistry And Enzymology), Fordham University, Bronx, New York, Michael J. Reale, Donald Dudley Clarke Phd, Walter J. Schubert, Friedrich F. Nord

Chemistry Faculty Publications

A young Metasequoia tree was debarked; its branches and heartwood were removed. The branches, sapwood and heartwood were separately ground to 8o mesh and air-dried. The moisture and lignin contents of these were determined. "Milled-wood" lignin was isolated from the sapwood sawdust, and was characterized by means of its ultraviolet and infrared absorption spectra. As a means of determining the empirical formula and the number of certain functional groups present in this lignin, an acetylated derivative and a phenylhydrazone were prepared. These were also studied spectroscopically. Elemental, methoxyl and acetoxyl analyses were performed on the original lignin and on its ...


Electron Capture Properties Of Halogenated Amine Derivatives / By Donald D. Clarke, Sherwin Wilk, And Stanley E. Gitlow, Donald Dudley Clarke Phd, Sherwin Wilk, Stanley E. Gitlow Jan 1966

Electron Capture Properties Of Halogenated Amine Derivatives / By Donald D. Clarke, Sherwin Wilk, And Stanley E. Gitlow, Donald Dudley Clarke Phd, Sherwin Wilk, Stanley E. Gitlow

Chemistry Faculty Publications

The use of gas-liquid chromatography (G.L.C.) for the analysis of amines of biological interest is currently under investigation in our laboratory. An intensive study of the chromatographic properties of a number of derivatives was presented by VandenHeuvel et al. (1), and this laboratory in a short communication reported on the possible use of heptafluorobutyrylated amine derivatives (2). As was noted in this early communication, sensitivity considerations must maintain priority in any proposed assay because of the extremely small quantities of these compounds present in biological fluids. For this reason, we have chosen to employ the electron capture detector ...


Compartmentation Of Glutamic Acid Metabolism In Brain Slices / Donald D. Clarke And Soll Berl Columbia Univ. School Of Medicine, N. Y. C., Donald Dudley Clarke Phd, Soll Berl Jan 1966

Compartmentation Of Glutamic Acid Metabolism In Brain Slices / Donald D. Clarke And Soll Berl Columbia Univ. School Of Medicine, N. Y. C., Donald Dudley Clarke Phd, Soll Berl

Chemistry Faculty Publications

The presence, in brain, of metabolic pools of glutamic acid have been demonstrated in vivo but not in tissue slices. Brain tissue slices prepared in the cold in Ringer's-bicarbonate containing 1% glucose and stored in an ice bath go not show compartmentation when incubated at 37 (10-20 min.) in a similar medium which contains tracer quantities of C aspartic acid, U.l.; the specific activity of glutamine remains considerably below that of glutamic acid. If such tissue slices are pre-incubated at 37° for 10 min. and then transferred to fresh medium containing radioactive tracer, after 10 min. at 37 ...


Automation Of The Assay For Transglutaminase / Donald D. Clarke And Ruth Nicklas, Donald Dudley Clarke Phd, Ruth Nicklas Jan 1966

Automation Of The Assay For Transglutaminase / Donald D. Clarke And Ruth Nicklas, Donald Dudley Clarke Phd, Ruth Nicklas

Chemistry Faculty Publications

Transglutaminase is an enzyme which catalyzes the Ca++-activated incorporation of amines into proteins. More detailed studies of the action of this enzyme showed that the incorporated amines displaced ammonia, and that only L-glutamine and not asparagine residues in the protein or peptide are substrates for this enzyme. This enzyme will not act on free glutamine, hence is not to be confused with glutaminase or transamidases which will act on free glutamine as a substrate. A variety of substituted glutamine peptides have been found to have substrate activity for this enzyme. Neidle and Acs, and more recently Folk and Cole ...