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At least 757 records · Page 42Linked to original sources
PubMed1978

Improved radiochemical assay for carnitine and its derivatives in plasma and tissue extracts.

We describe the measurement of carnitine and short-chain and long-chain acylcarnitines in perchloric acid extracts of liver and muscle. [1-14C]Acetyl-CoA is used, and labeled acetylcarnitine is measured with a sensitivity of less than 1 to 50 nmol of L-carnitine per 50-microliter sample. Samples frozen at -20 degrees C lost no carnitine during several months. Analytical recovery of carnitine (5 nmol) added to 50-microliter perchloric acid extracts of liver was 103 +/- 2%. This method may be suitable for clinical applications such as screening patients with muscle and metabolic disorders.

Acetylcarnitine↗
PubMed1981

Improved method for confirmation of identity of aflatoxins B1 and M1 in dairy products and animal tissue extracts.

A method is described for confirming the identity of aflatoxins B1 and M1 in dairy products and liver extracts on a thin layer plate. Extracts and standards containing aflatoxins B1 and M1 are spotted on 10 x 10 cm plates, which are developed 2-dimensionally in mixtures of isopropanol-acetone-chloroform. After the first development, trifluoroacetic acid-hexane (1 + 4) is sprayed on that part of the plate containing the separated extract components and the underdeveloped standard spots of B1 and M1, and the plate is heated 6-8 min at 75 degrees C. Then the plate is developed in a second direction, and the reaction products of B1 and M1 with trifluoroacetic acid from the extract are compared with the same derivatives of the respective standards. The method has been used successfully on extracts of milk, cheese, and liver containing 0.1 ng B1 or M1/g and can be completed in 35-45 min.

Aflatoxin B1↗
PubMed1993

Quantification of p53 protein in tumor cell lines, breast tissue extracts and serum with time-resolved immunofluorometry.

We have developed a highly sensitive time-resolved immunofluorometric procedure for quantifying mutant or wild-type, human or murine, p53 protein. The method uses monoclonal PAb240 or PAb421 antibodies for capture and a polyclonal rabbit antibody for detection. The final immunocomplex is quantified with an alkaline phosphatase substrate which, when hydrolyzed by the enzyme, forms highly fluorescent long-lived complexes with Tb(3+)-EDTA. The detection limit is approximately 1 pg of protein per assay. The assay was applied for the quantification of p53 protein in lysates from 23 cell lines and overproducers of mutant protein were identified. Eight hundred cancer patients sera tested negative for the presence of p53. We have also applied the quantitative immunofluorometric procedure for measuring mutant p53 protein in breast tumor extracts specifically prepared for steroid hormone receptor analysis. Sixty-four out of the 264 extracts (24%) were positive for p53. Significant negative correlations between levels of p53 and steroid hormone receptors were found. The proposed analytical methodology simplifies the assessment of p53 status in tumor extracts, has many advantages over immunohistochemical techniques and is proposed as a method of choice for routine clinical use and other investigations involving p53.

Animals↗
PubMed1983

Epidermal growth factor is not the major growth-promoting agent in extracts of prostatic tissue.

Extracts of benign prostatic hyperplasia (BPH) contain a factor which is mitogenic for human foreskin fibroblasts in culture. Because of the similarity of BPH extract and epidermal growth factor (EGF) in stimulating quiescent fibroblasts to divide, it was of interest to determine if the prostate-associated growth factor competes for EGF receptor binding. BPH extract was found to compete poorly for 125I-EGF-receptor binding, did not influence the dissociation of cell-bound 125I-EGF and caused only a slight down-regulation of the EGF receptor. These findings indicate that EGF and BPH extract do not recognize the same receptor and that the major growth stimulating activity of BPH extract is not due to EGF.

Binding, Competitive↗
PubMed1986

Selective osteoblast mitogens can be extracted from prostatic tissue.

Extracts of human prostatic carcinoma and of human benign prostatic hyperplasia were found to exhibit mitogenic activity in freshly isolated rat osteoblasts, rat fibroblasts, and osteoblast-derived osteosarcoma cells. This activity was markedly reduced by tryptic digestion of extracts, indicating its protein nature. Results of bioassay studies suggested that the prostatic material was different from a number of known growth factors. Analysis by reversed-phase high performance liquid chromatography revealed that extracts contained mitogenic activity for osteoblasts that was distinct from fibroblast-stimulating activity. Such osteoblast growth factors could form the basis of the skeletal osteogenic response to metastatic prostatic adenocarcinoma.

Adenocarcinoma↗
PubMed1981

Immunological characterization of cytochrome b9 in crude extracts from rat tissues.

Rabbit antiserum against rat liver-soluble cytochrome b9 was produced. The antiserum was specific to cytochrome b9 and did not react with hemoglobin, cytochrome c, cytochrome H-450, serum, hemolysate, and tissue extracts from lung, brain, testis, and skeletal muscle. From Ouchterlony double immunodiffusion and tandem crossed immunoelectrophoresis, the antigen was found in liver, kidney, and heart tissue extracts of rat with complete identity. From crossed immunoelectrophoresis, the antiserum distinguished monomeric and dimeric forms of the antigen. Rocket immunoelectrophoresis for quantitating the antigen was developed with a minimum sensitivity of 5 ng. By using rocket immunoelectrophoresis, the concentration of the antigen in crude tissue extracts from liver, heart, and kidney was determined. The antigen was not detectable in crude extracts from lung, brain, testis, and skeletal muscle by immunological methods. Therefore, the immunological assay method was very useful for identifying and quantitating cytochrome b9 in crude extracts with high sensitivity.

Animals↗