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Biomedical subjects

J Kroll

Publications and source records attributed to J Kroll.

At least 91 records · Page 5Linked to original sources
PubMed1976

DNA-binding proteins in Yoshida ascites tumor fluid.

DNA-binding proteins were isolated from Yoshida ascites tumor fluid by chromatography on DNA-cellulose. This fraction represents 1-2% of the total ascites protein. Most of the DNA-binding proteins will bind to phosphocellulose as well. The proteins migrate by agarose gel electrophoresis at pH 8.6 as alpha and beta globulins. Quantitative immunoelectrophoresis revealed the presence of 12-18 proteins. SDS-polyacrylamide electrophoresis indicated molecular weights ranging from 3-10(4) to 10(6). Seven of the proteins were identified by specific immunoprecipitation as beta1-Eglobulin, beta2-glycoprotein I, fibrinogen split product E (fibrinogen E), coagulation factor XIII (factor XIII), alpha2-macroglobulin, IgG and IgM. Alpha1-antichymotrypsin might also be represented. In nuclear extracts of the tumor cells only factor XIII was present. With the exception of fibrinogen E and P5 all recognized DNA-binding proteins are present in normal rat plasma. With increasing tumor age the concentration of fibrinogen E, factor XIII, P5 and IgM increased both in ascites fluid and in plasma, while the concentration of other DNA-binding-proteins decreased or remained constant. Evidence is presented that the DNA- and phosphocellulose binding ascites protein fraction inhibit tumor cell growth. No inhibition was induced by corresponding protein fractions isolated from normal rat plasma.

Animals↗
PubMed1976

Specific antisera produced by immunization with precipitin lines.

Individual plasma proteins were precipitated, identified and isolated on the basis of line immunoelectrophoresis. A monospecific antibody response was induced by immunization of rabbits with less than 50 ng of precipitated antigen. Preservation of monospecificity was obtained by reimmunization with precipitates developed against the specific antisera.

Animals↗
PubMed1976

Protein composition in the fluid of individual bovine follicles.

The proteins in follicular fluid from individual and pooled bovine follicles were studied by gel chromatography and quantitative immunoelectrophoresis. The mean protein concentration was 86-4% of serum; very large proteins were present in only low concentrations. A minimum of 40 individual proteins was distinguished in follicular fluid, and 15 of these proteins were quantitated. A correlation between molecular weight and follicular fluid: serum concentration ratio was found. Fluid from individual follicles differed only in the relative concentrations of small and large proteins. An exception to this was IgG which was occasionally, but never in healthy growing follicles, present in concetrations above 150% of serum. Healthy growing, preovulatory and atretic follicles had higher, and cystic follicles mostly lower, concentrations of small proteins than serum. The concentration of alpha2-macroglobulin in healthy growing follicles never exceeded 16% of serum. The concentration of large proteins in follicular fluid increased with increasing follicle size. Attempts to detect proteins specific to follicular fluid by immunizing rabbits with pooled follicular samples and the follicular fluid proteins not bound by anti-bovine antiserum resulted in production of antibodies against fibrinogen and its split products D+E only.

Albumins↗
PubMed1976

[Measurement of emulsion stability].

For the routine assessment of the stability of water-in-oil emulsions, the authors suggest to determine the beginning of de-emulsification or to measure the stability constant at 38 degrees C., since these methods yield fairly reproducible results and require but little time and laboratory outfit. More accurate results will be obtained only by conductance measurements.

Chemical Phenomena↗
PubMed1975

Identification of immunoprecipitates in line immunoelectrophoresis.

A technique has been developed for the identification of immunoprecipitates in complex line-immunoelectrophoretic patterns. It is based on localized adsorption of individual antigens by monospecific antisera. The technique is suited for the following purposes as well: (1) testing the specificity and titer of uncharacterized antisera and (2) evaluation of binding properties of chromatographic media.

Antibody Specificity↗
PubMed1975

[Simultaneous isolation of proteins and fats from oil seeds. I. Principle of procedure].

The principle of the procedure for the simultaneous isolation of proteins and fats from oil seeds is illustrated by the isolation of these constituents from sunflower seeds. This procedure is based on the displacement of oil and the extraction of protein by an aqueous electrolyte solution after comminution of the pretreated seeds, removal of the insoluble cell components and separation of the extracts into a fat-containing and a protein-containing phase. The globulins are precipitated isoelectrically; the albumins, by using complexing agents or thermal coagulation. The liberation of the oil from the concentrated fat emulsion is achieved immediately in a mechanical way or after addition of destabilizers. The results are discussed with regard to the yields obtained and the composition of the final products.

Albumins↗