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Biomedical subjects

C R Shaw

Publications and source records attributed to C R Shaw.

35 records · Page 2Linked to original sources
PubMed1971

Comparative zone electrophoresis of enzymes of Pseudomonas solanacearum and Pseudomonas cepacia.

The technique of starch-gel electrophoresis with specific staining for a series of enzymes was used to compare 21 Pseudomonas strains representing both P. cepacia and P. solanacearum. These experiments produced no evidence for close similarity of the two species. Twelve strains of P. solanacearum were compared by means of data obtained from nine different enzymes, and the data indicate that these strains belong in two biotypes. Except for the assignment of two strains, these groups are the same as the two major groups previously derived from nutritional properties and from deoxyribonucleic acid hybridization experiments. Eleven enzymes were available for comparisons of the P. cepacia strains. Eight of these strains form a homogeneous group, but the last strain, number 249, differs considerably from the other representatives of the species.

Alcohol Oxidoreductases↗
PubMed1969

Zone electrophoresis of enzymes in bacterial taxonomy.

The electrophoretic mobilities in starch gels have been determined for eight enzymes in extracts of representative cultures of members of the family Enterobacteriaceae. These values were compared with each other and with those obtained from certain bacteria not in this family. The migrations of the eight enzymes were virtually identical for each of eight strains of Escherichia coli and for two species of Shigella. A number of these enzymes appeared to be identical in other organisms believed to be closely related to E. coli (Salmonella), and the number of differences increased in organisms which appeared to have lesser degrees of relatedness by other criteria (deoxyribonucleic acid base compositions, overall similarity).

Alcaligenes↗
PubMed1966

Glucose-6-phosphate dehydrogenase: homologous molecules in deer mouse and man.

Two forms of glucose-6-phosphate dehydrogenase, A and B, have been reported in deer mouse tis sues. The B enzyme, which showed autosomally controlled polymorphism, is now found to be equally active to ward glucose-6-phosphate and galac tQse-6- phosphate; the A enzyme is specific for the former. Human and horse livers also have two forms of glucose-6-phosphate dehydrogenase which exhibit the same substrate spe cifities as those in the deer mouse. A wide variety of electrophoretic patterns was seen in the human galactose-active enzyme.

Animals↗