Binding of lysozyme to common pili of Escherichia coli.

Common pili from Escherichia coli were found to bind hen egg white lysozyme. The binding was highly dependent on ionic strength, and the maximum binding occurred near an ionic strength of 0.02.

Structure of common pili from Escherichia coli.

Several important properties of the common pili from Escherichia coli are discussed. These pili were resistant to the gentle Folin-Ciocalteau reagent methods for protein detection and were not readily solubilized by sodium dodecyl sulfate. They were found to contain a reducing sugar but not peptidoglycan.

Fats and atheroma: an inquest.

All well-controlled trials of cholesterol-reducing diets and drugs have failed to reduce coronary (CHD) mortality and morbidity. Nevertheless, commercial, professional, and even government-sponsored propaganda continues. Experimentally some vegetable oils and hardened fats can be more damaging to arteries than butter.

Glycoproteins of natural origin with an affinity for hepatitis B surface antigen.

Sera from certain animal species contain a substance(s) which binds hepatitis B surface antigen. The hepatitis B binding substance found in animals is not antibody, but appears to be a glycoprotein which reacted with antigen-coated beads and produced a "false positive" test for antibody. This glycoprotein could be selectively and quantitatively removed by reaction with purified hepatitis B surface antigen and centrifugation.

Metal ion dependence of a heat-modifiable protein from the outer membrane of Escherichia coli upon sodium dodecyl sulfate-gel electrophoresis.

One heat-modifiable protein of Escherichia coli outer membrane does not completely change to the high-temperature form in the presence of magnesium ion in sodium dodecyl sulfate solution. When the metal ion complexing reagents ethylenediaminetetraacetic acid, phosphate ion, hydroxyl ion, or the competitive cations Zn2+ or Ca2+ are added to the sodium dodecyl sulfate-solubilized sample of outer membrane, and then the sample is heated to 100 degrees C and recooled to room temperature, the protein is almost completely converted to the high-temperature form. In control samples, or if sodium chloride, magnesium chloride, or manganous chloride are added to these samples and treated the same way, a large amount of the low-temperature form of the protein is preserved.

Experimental parainfluenza type 1 virus-induced encephalomyelopathy in adult mouse: a histopathological study.

The pathogenicity of a strain of parainfluenza type 1 virus, isolated from the cultured brain cells from multiple sclerosis patients and designated as 6/94 virus, was studied in mouse brain. Selective degeneration of cerebral white matter, preceded by mononuclear cell infiltration, and ependymitis were prominent pathological features of the mouse intracerebrally inoculated with 6/94 virus. After inactivation by ultraviolet light the virus was still capable of producing the inflammatory and degenerative white matter lesions, although the severity of ependymitis was substantially reduced.