Search PubMed⌕ Search

Biomedical subjects

T A Baker

Publications and source records attributed to T A Baker.

60 records · Page 4Linked to original sources

Mu dX, a derivative of Mu d1 (lac Apr) which makes stable lacZ fusions at high temperature.

We describe defective Mu phage Mu dX (Mu d1 Bx::Tn9 [lac Apr Cmr]) which is useful for insertion mutagenesis and for construction of lac operon fusions in vivo. Mu dX retains the insertion properties of Mu d1 but produces temperature-resistant lysogens and transposes at a reduced frequency. A method is described to convert existing Mu d1 insertions to Mu dX.

Bacteriophage mu↗

Regulation of short-term changes in hepatic beta-hydroxy-beta-methylglutaryl-CoA reductase activity.

Immunotitrations of rat liver hydroxymethylglutaryl-CoA (HOMeGlt-CoA) reductase activity were performed before and after short-term changes in the nutritional or hormonal state of the animals. Changes in enzyme activity (increase or decrease) within 1 h following cholesterol feeding or glucagon or mevalonolactone administration to normal rats, or insulin administration to diabetic rats were accompanied by no change in the specific activity of the enzyme, as determined from the quantity of enzyme activity inactivated by a fixed quantity of antibody. These results support the conclusion that the loss in enzyme activity was due to conversion of the enzyme to immuno-unreactive products. In agreement with this conclusion the enzyme activity lost after these short-term physiological changes was not restorable by phosphoprotein phosphatase action. On the other hand, incubation of rat liver microsomes with ATP and Mg2+ decreased the specific activity of HOMeGlt-CoA reductase about tenfold, as determined by immunotitration. The low specific activity produced under these conditions was increased by phosphatase action to nearly the original level. The above evidence suggests that the changes in HOMeGlt-CoA reductase activity that resulted from short-term physiological changes in hormonal or nutritional states of an animal were brought about by a change in the quantity of enzyme, and not by reversible phosphorylation of pre-existing enzyme.

Animals↗

Ectopic immature renal tissue over the dorsum of lumbar and sacral area in two infants.

During reparative surgery for meningomyelocele of the lumbar area, a 7-week-old female infant was found to have a small, well-delineated, subcutaneous, renal blastema. A 3-month-old female infant was found to have immature renal tissue, consisting of glomeruli and tubules, in a soft tissue swelling dorsal to the sacrum. Neither of these patients showed neurologic or renal abnormalities. The second patient has had a disease-free follow-up period of six years. The possible etiology and significance of these benign findings and their relation to the origin of Wilms tumors are discussed.

Choristoma↗

Toxicology of various pesticides and their decomposition products on mitochondrial electron transport.

The effect of various pesticides and derivatives on mitochondrial electron transport systems was assessed. DDT, DDE, TDE, Kelthane, chlorobenzilate, chloropropylate and Acarol were found to be inhibitory towards both heavy beef heart mitochondrial (HBHM) NADH-oxidase and succinoxidase enzyme systems. Dichlorobenzophenone and p-chlorophenol were less inhibitory towards the HBHM NADH-oxidase and did not inhibit the succinoxidase enzyme system. DDA did not inhibit either of the electron transport systems. Carbaryl was not inhibitory towards both HBHM oxidase systems, whereas its degradative product dihydroxynaphthalene was inhibitory at the same concentration. Furadan, Matacil, Baygon and Dimetilan were only slightly inhibitory towards themitochondrial NADH-oxidase system and did not inhibit the succinoxidase system. Zectran was inhibitory towards the NADH-oxidase system and was not inhibitory towards the succinoxidase system. DDT, DDE and TDE, dihydroxynaphthalene and 1-naphthol inhibited the NADH-oxidase enzyme system onthe substrate side of cytochrome c, whereas Kelthane inhibited on the oxygen side.

Animals↗