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Biomedical subjects

L Levine

Publications and source records attributed to L Levine.

At least 361 records · Page 20Linked to original sources

Differentiated rat glial cell strain in tissue culture.

Rat glial tumors, induced by injections of N-nitrosomethylurea, were plated and propagated in culture. Among a few cell strains obtained, one clone contains S-100 protein, which is unique to brain in vertebrates. Stationary-phase cultures contain approximately ten times more S-100 protein per cell than exponentially growing cells. When injected into newborn rats, cells producing S-100 grew as a glial tumor, which contained S-100 protein.

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Complement-inactivating proteinase(s) from Clostridium histolyticum.

A proteinase fraction inhibiting the hemolytic activity of guinea pig complement was obtained from supernatant fluids of Clostridium histolyticum cultures and purified 150- to 350-fold by ammonium sulfate precipitation, Sephadex G-75 gel filtration, and diethylaminoethyl cellulose chromatography. An assay was developed based on the inactivation of hemolytic complement. Partially purified anticomplementary preparations were active against casein and were capable of "solubilizing" Escherichia coli endotoxin. Two components were found by differential heat inactivation, with complement and casein as substrates, but only one of these components was active against endotoxin. The more heat-stable activity, showing 50% inactivation at about 47 C, was characterized as to pH and ionic strength optima and sensitivity to reagents such as cysteine, beta-mercaptoethanol, ethylenediaminetetraacetate, and heavy metals.

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Characterization of a human serum inhibitor of Clostridium histolyticum proteinase(s).

Normal animal sera inhibit at least one Clostridium histolyticum proteinase. An assay procedure based on immune hemolysis was developed for the estimation of this inhibition. This inhibitory activity occurs in various levels in the sera of different animal species. The highest titers have been obtained with rat sera. The inhibitory activity from human serum was isolated and purified 16- to 27-fold by Sephadex G-200 gel filtration and diethylaminoethyl cellulose or hydroxylapatite chromatography. The properties of the human serum inhibitor of the clostridial proteinase were compared with a trypsin inhibiting factor found in the partially purified preparations. Identical behavior of the two inhibitory factors was observed when measured by heat inactivation, beta-mercaptoethanol sensitivity, pH stability, and sucrose gradient centrifugation. The inhibitory factor has an approximate sedimentation coefficient (S(20,w)) of 17. Goat anti-alpha-2-macroglobulin specifically precipitated the clostridial proteinase inhibitor from a partially purified preparation.

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The serologic specificity of tropocollagen telopeptides.

Tropocollagen preparations from carp, buffalo fish, rats, calves, sheep, and humans have been studied by electron microscopy and serologic methods. Tropocollagens from each species appeared identical by electron microscopy but they were readily distinguished (except between sheep and calves) by C'-fixation tests with rabbit antisera against the various tropocollagens. Tests with calf tropocollagen antiserum showed no distinction between tropocollagen isolated from different tissues nor between individuals of the same or different strains. The major immunogenic sites in native tropocollagen are the telopeptides, and these are present on both alpha1- and alpha2-chains. The C'-fixing activity was lost with heat denaturation of the tropocollagen, but could be recovered in a concentration-dependent process on cooling. The fact that pure and enzyme-treated collagen can provoke serologic reaction implies that collagenous sutures and prostheses used in surgery may lead to sensitization and rejection, a fact which may merit clinical concern.

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