Effect of the type of diet on the distribution of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase in rat small intestine

Summary The jejunoileal gradient for the HMG-CoA reductase activity in the microsomal fraction of the epithelial cells of the small intestine of rats given commercial pellets was reserved within a few days after changing the ration to a semipurified diet. The response of the reductase was essentially the same in villus and crypt cells.     

Local aggregation of hormone-receptor complexes is required for activation by epidermal growth factor.

An analogue of epidermal growth factor (EGF) which is virtually devoid of biological activity retains receptor binding activity but cannot form cell surface clusters or patches. Bivalent anti-EGF antibodies restore both bioactivity and patch formation. The sensitivity of fibroblasts to native EGF can also be enhanced greatly by these antibodies, especially in hormone-resistant cell lines.     

Persistence of orientation-selective cells of the primary visual cortex in kittens enucleated unilaterally at birth and reared in darkness]

In kittens dark reared (6 weeks old) orientation selective cells are no longer recorded in the primary visual cortex, while in kittens of same age, enucleated at birth unilaterally and reared in identical conditions, 30% of visual cortical cells are shown to be orientation selective and in addition respond preferentially to horizontal and vertical orientations.     

Unusually strong lipophilicity of ‘fat’ or ‘super’ amino-acids,including a new reference value for glycine

Summary Lipophilic, steric, electronic, and enzyme resistance characteristics of carboranylalanine, adamantylalanine, neopentylglycine and tert-butylglycine are described. The first 2 amino-acids display lipophilicities 2 orders of magnitude higher than tryptophan.This work was supported by research grants to Prof. R. Schwyzer from the Swiss National Science Foundation.     

Occurrence of thiaminase II in Saccharomyces cerevisiae

It was found that cell-free extracts of Saccharomyces cerevisiae contain thiaminase II which hydrolyzes thiamine and thiamine analogs. The possible involvement of this enzyme and thiamine-synthesizing enzymes in thiamine production from thiamine antagonists is discussed.