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Biomedical subjects

B Schiller

Publications and source records attributed to B Schiller.

At least 55 records · Page 3Linked to original sources
PubMed1979

Stability of the lyophilized F(ab')2 fragments of horse tetanus antibodies isolated by affinity chromatography.

F(ab')2 fragments of horse tetanus antibodies were obtained from horse hyperimmune sera after peptic digestion. The digest was passed through a column of tetanus toxoid coupled with Sepharose 4B, F(ab')2 fragments were eluted with a solution of 5 mM HCl in 150 mM NaCl and the eluates were concentrated by ultrafiltration and lyophilized. Glycine and human serum albumin were used as stabilizing agents. Polyacrylamide gel electrophoretic mobility and molecular weight of the fragments remained unchanged after lyophilization. Freeze-dried preparations stored two months at 56 degrees C showed only a slight decrease in antitetanus activity. The ORD measurements and spectrophotometric determinations of unfolding over pH range 2.1-5.0 show that the F(ab')2 fragment structure is highly stable in acid medium.

Animals↗
PubMed1977

Purification of Clostridium toxoids.

A two-step fractionation procedure was applied for purification and concentration of the individual Clostridium toxoids. The toxoids were precipitated with hydrochloric acid in the presence of sodium sextametaphosphate, then antigenic fractions were separated from inactive contaminants by Sephadex G-75 filtration. Specific activity of the preparations thus obtained, as determined by Mancini radial immunodiffusion, was 150--565 binding units per mg of protein nitrogen for Clostridium perfringens toxoid, 204--352 binding units for Clostridium oedematiens toxoid and 26.6 -- 51.2 binding units for Clostridium septicum toxoid.

Clostridium↗
PubMed1976

A versatile method for purification of diphtheria toxoid for immunization purposes.

Diphtheriae growth supernatant. The toxoid was quantitatively recovered from the immunosorbent in two fractions: the first in 0.005 M hydochloric acid and the second in 6' M urea containing 0.1 M HCL. Both fractions were soluble in aqueous solvents, and both had a similar specific activity: between 200 and 250 Lf/mg protein, and about 1.5 protective unit (ED50) per l Lf unit, as assayed in guinea pigs. Using the same procedure, the specific activity of a commerical toxoid preparation, purified and concentrated, was increrased two fold, from 130 Lf/mg to 260 Lf/mg protein.

Animals↗
PubMed1975

Circular DNA and rolling circles in nucleolar rDNA from mitotic nuclei of Physarum polycephalum.

1. About 15% of nucleolar DNA (1.712 g/cm3) from Physarum polycephalum displaying maximum hybridization to ribosomal RNA, is composed of circular DNA of 3.9 +/- 0.2 mum contour length or multiples thereof. 2. A portion of these circular molecules (25%) contained linear DNA pieces longer than circumference length. In a small fraction of circular DNA linear pieces, shorter than the unit length, were observed. 3. Most nucleolar DNA, [3H]thymidine-labeled or hybridizable to ribosomal RNA was separable from chromosomal DNA during G2 phase, mitosis and S phase of the cell cycle. 4. Ribosomal DNA content was not amplified during the cell cycle, was unchanged during exponential or stationary growth phase and amounted to about 0.11 -- 0.21% of nuclear DNA in diploid and hexaploid strains of Physarum or 100--200 ribosomal genes per diploid genome.

Cell Division↗
PubMed1975

Lipid accumulation in smooth muscle cell lysosomes im primate atherosclerosis.

Cytochemical and ultrastructural examination of the developing atherosclerotic lesion in hypercholesterolemic rhesus monkeys reveals that lipid is sequestered within lysosomes of aortic smooth muscle cells. A common pathway in the development of sclerotic arterial disease appears to be overloading of vascular smooth muscle cell lysosomes with a variety of metabolites. This may occur as a consequence of an excess of substrate or because of a congenital deficiency of a lysosomal hydrolase.

Animals↗
PubMed1973

Lysosomes in aortic smooth muscle cells. Effects of hypertension.

Hypertension induces hypertrophy and increased turnover of aortic smooth muscle cells along with an accumulation of connective tissue in the aortic wall. We identified the lysosomes in normal and hypertensive aortic muscle cells by light and electron microscopy, utilizing cytochemical staining for acid phosphatase activity. Lysosomes were found to be more numerous in hypertensive vessels. Biochemical assays of two specific lysosomal enzymes revealed a doubling of acid phosphatase and a more than threefold increase in beta-N-acetyl-glucosaminidase activities in hypertensive aortas.

Acid Phosphatase↗