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Biomedical subjects

M D Scawen

Publications and source records attributed to M D Scawen.

50 records · Page 3Linked to original sources
PubMed1983

Evaluation of an enzymic procedure for the measurement of acetaminophen.

We evaluated a new method for measurement of acetaminophen. From acetaminophen, acetate and p-aminophenol are enzymically produced, and the latter product is determined colorimetrically by reaction with o-cresol and ammoniacal copper sulfate. The method is rapid and precise, and results compare well with those by spectrophotometric and liquid-chromatographic techniques. Major metabolites of acetaminophen, some commonly used drugs, or phenolic substances that may be present in patients with liver or renal disease do not interfere.

Acetaminophen↗
PubMed1982

The rapid purification of 3-hydroxybutyrate dehydrogenase and malate dehydrogenase on triazine dye affinity matrices.

3-Hydroxybutyrate dehydrogenase (EC 1.1.1.30) and malate dehydrogenase (EC 1.1.1.37) were purified to homogeneity on a large scale involving only two sequential affinity-chromatography steps on two triazine dye-Sepharose matrices. Recoveries of both enzymes were in excess of 60%. Malate dehydrogenase could also be purified by a combination of triazine dye affinity chromatography and gel filtration on Ultrogel AcA-44, but this offered no significant advantage over the purely affinity procedure.

Chromatography, Affinity↗
PubMed1975

The amino acid sequence of plastocyanin from spinach. (Spinacia oleracea L.).

The amino acid sequence of spinach (Spinacia oleracea L.) plastocyanin was determined. It consists of a single polypeptide chain of 99 residues and has a sequence molecular weight of 10415. The sequence was determined by using a Beckman 890C automatic sequencer and by the dansyl--phenyl isothiocyanate analysis of peptides obtained by the enzymic digestion of purified CNBr fragments. Overlap through the two methionine residues was not shown. Sedimentation equilibrium in the ultracentrifuge gave a molecular weight for spinach plastocyanin of about 9000, in contrast with the value of 21000 reported previously by Katoh et al. (1962).

Amino Acid Sequence↗
PubMed1974

The amino acid sequence of plastocyanin from Solanum tuberosum L. (potato).

The amino acid sequence of plastocyanin from potato was determined. It consists of a single polypeptide chain of 99 residues, of molecular weight 10332. The sequence was determined by using a Beckman 890c sequencer and by dansyl-Edman analysis of peptides derived from purified CNBr fragments. The sequence shows considerable similarity with that of Chlorella fusca, and also with the C-terminal region of bacterial azurins.

Amino Acid Sequence↗
PubMed1974

The amino acid sequence of plastocyanin from Vicia faba L. (broad bean).

The amino acid sequence of plastocyanin from broad bean was determined. It consists of a single polypeptide chain of 99 residues. The sequence was determined by using a Beckman 890C sequencer and by dansyl-phenyl isothiocyanate analysis of peptides obtained by the enzymic cleavage of purified cyanogen bromide fragments. Some parts of the sequence depend on the results of Edman degradation of peptides for which amino acid analyses were not obtained. The evidence for one overlap is not strong.

Amino Acid Sequence↗
PubMed1974

The amino acid sequence of plastocyanin from Cucurbita pepo L. (vegetable marrow).

The amino acid sequence of plastocyanin from marrow was determined. It consists of a single polypeptide chain of mol.wt. 10284 containing 99 amino acid residues. The sequence was determined by using a Beckman 890C automatic sequencer and by dansyl-phenyl isothiocyanate analysis of peptides obtained by the enzymic digestion of purified CNBr fragments. The sequence is in good agreement with the amino acid composition, except that fewer residues of glutamic acid were found in the sequence than were suggested by the composition. Evidence for histidine-37 was weaker than for the rest of the sequence. A ;tree' of phylogenetic affinities was constructed by using several higher-plant plastocyanin sequences.

Amino Acid Sequence↗
PubMedDate not supplied

Gold-resistant bacteria: excretion of a cystine-rich protein by Pseudomonas cepacia induced by an antiarthritic drug.

P. cepacia bacteria adapted to growth in a chemically defined medium containing millimolar concentrations of Au(I) thiolates including the antiarthritic drug Au(I) thiomalate. The bacteria became very large, accumulated polyhydroxybutyrate and gold, and excreted a yellow protein ("thiorin"), which caused foaming of the culture medium. Thiorin was shown by 1H-NMR, amino acid analysis, and gel filtration chromatography to be of low molecular weight (ca. 9500) and to contain predominantly Cys (oxidized), Glx, and Gly.

Bacterial Proteins↗