[Total parenteral nutrition in cancer patients].
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Biomedical subjects
Publications and source records attributed to A Conti.
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Protein metabolism may be upset dramatically by several pathological condition such as starvation, malnutrition, surgical stress. Serum proteins have been investigated in many works but very few studies exist about muscle and organ proteins. This article describes two methods for extraction of muscle water soluble proteins: a macromethod that uses some hundred grams of tissue, and a micromethod that starts from a little muscle biopsia. Extracts have been tested for protein content by electrophoresis on cellulose acetate and isoelectrofocusing on polyacrylamide gel and have shown a rich variety of protein fractions.
A new preparation technique to raise rabbit antisera against human water-soluble muscle proteins is presented. Immunization, blood collection and further purification of antibody fraction in serum are described in detail. The present method is fast and easy to perform; chromatography and dialysis are not required and antisera so produced lend themselves to immunoelectrophoretic evaluation of human water-soluble muscle proteins.
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A CSF electrophoresis on a particular gelatinized cellulose acetate (Cellogel RS) has been tested. The method allows the routine separation of many protein fractions in concentrated CSF in a very brief time and affords the recognition and quantification of oligoclonal banding, that is of extreme importance in the diagnosis of some neuropathies as multiple sclerosis.
The mammary secretions of a monogastric, the ass, and those of a Tylopode, the camel (camelus dromedarius), were examined by double diffusion in agarose gel against rabbit sera anti-bovine beta-lactoglobulin. Clear precipitin reactions were obtained. After immunoelectrophoresis the camel and she-ass beta-lactoglobulins showed very different electrophoretic mobilities.
An improved technique of two dimensional immunoelectrophoresis of serum proteins on gelatinized cellulose acetate for routine evaluation of protein nutritional state is described. The method, which allows the estimation of more than 30 protein fractions, proves extremely useful in monitoring the effectiveness of total parenteral nutrition and protein metabolic conditions. Sera samples from healthy subjects and cachectical neoplastic patients have been examined and preliminary results are reported.
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By double diffusion in agarose gel, in well defined experimental conditions, cross reactions were observed between porcine beta-lactoglobulins and anti-bovine beta-lactoglobulin antisera. The immunological reactivity between these beta-lactoglobulins from a monogastric and the ruminant anti beta-lactoglobulin antiserum thus implies a certain degree of similarity between the monomeric beta-lactoglobulins examined and the dimeric of the ruminants. With the same antisera it also proved possible to demonstrate the presence of beta-lactoglobulins in the mammary secretions of another monogastric, namely, the mare. Identity reactions observed between sow's and mare's beta-lactoglobulins seem to indicate a close similarity in their structures.
Over thirty specimens of breast milk and colostrum were examined by the double diffusion method in agarose gel using antibovine beta-lactoglobulin antisera. Cross reactions were obtained showing the presence of beta-lactoglobulins in human milk and colostrum; the strength of these reactions was comparable with those already observed with porcine and equine mammary secretions. Identity reactions were obtained between human and sow's milk against anti-bovine beta-lactoglobulin antisera. Results are discussed from the immunological and structural point of view.
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The authors explored the gastric function of 20 volunteers by classical methods and by the assessment of gastric 99Tc pertechnetate clearance. From a comparison of results obtained with the various methods they come to the conclusion that the pertechnetate clearance method is dependable, easy to perform, and noninvasive; accordingly, they recommend its use as the method of choice for monitoring the treatment of duodenal ulcers and evaluating its results.
SHBG (sex hormone binding globulin) is a carrier protein for the sex hormones testosterone and estradiol with a molecular weight of about 95000 dalton. It can be used as a metabolic test of thyroid function. SHBG was measured by the adsorption method of Mickelson and Petra; the SHBG contained in serum is incubated with 3H-5alpha-dihydrotestosterone and adsorbed to a cellulose filter. Thirty-eight female patients with hyperthyroidism before treatment had markedly elevated levels of SHBG (x +/- SD: 4.85 +/- 2.4 microgram DHT/100 ml) compared with normal controls (1.50 +/- 0.57; p is less than 0.001). A good correlation between the thyroid hormones and SHBG could be domonstrated which was better for T3 than for T4:r =0.76 (p is less than 0.001) for T3 and r= 0.65 (p is less than 0.001) for T4. This agrees with the clinical finding that the circulating T3 level is a better index of the metabolic severity of thyrotoxicosis than T4. After radioiodine treatment SHBG returns to normal values in euthyroid patients (1.38 +/- 0.8; n = 15) and remains elevated in persistent hyperthyroidism (3.99 +/-1,6; n = 67). Even in patients with persistent biochemical hyperthyroidism who are completely euthyroid on clinical examination, SHBG remains high. Despite lack of evidence of clinical hyperthyroidism, this metabolic test demonstrates the biologic significance of merely biochemical hyperthyroidism. Estimation of SHBG as a metabolic thyroid function test in vitro is of special value for the evaluation of patients showing discrepancies between the clinical and biochemical states and for borderline hyperthyroidism.
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