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[Stress-induced blood protein and blood lipid changes and their dependence on learning and conditioning].

Rats were subjected to two kinds of stress and consequent changes in blood protein and lipids were investigated. Furthermore, an attempt was made to ascertain whether or not increases or decreases in these blood parameters were reproducible by conditioning. In the first experiment animals were subjected to stress in a modified running wheel (Noble Collip drum). A series of 10 conditional stimuli (light-sound combined) was delivered together with the stress-producing stimulus. After the first exposure to stress a relative alpha1-globulin increase was observed. After 10 stress exposures the hitherto neutral stimulus alone produced a conditioned increase in the alpha1-globulin fraction. The gamma-globulin values were decreased after the first exposure to stress, but increased after 10 stress exposures. This increase could also be conditioned. In the second experiment "white noise" stress was used (110 dB). The conditional stimulus was light. After short exposure to the stress-inducing stimulus, the gamma-globulins showed a slight drop and remained thus during the whole experiment. The analysis of blood lipids showed increased stress values for alpha-lipoprotiens and reduced values for beta-fractions. Cholesterol and triglycerides reacted like the beta-lipoproteins. The total blood lipid content was, however, increased. The conditioned increase in alpha-lipoproteins and total lipids was statisticallysignigicant. It is noteworthy that the conditioned alpha-lipoprotein levels shoeed significant differences between experimental and control groups. The conditioned stress increased the levels of cholesterol and triglycerides, whereas under real stress conditions decreases were found. Research on "conditioned stress" could beof improtance in regard to clinical aspects of coronary heart disease.

Animals

Interaction of synthetic human big gastrin with blood proteins of man and animals.

Radio gel and affin chromatography were used to study big gastrin interaction with blood proteins of man and animals. The experiments showed that big gastrin interacts with serum proteins in vitro. The gastrin-blood protein complex is labile and readily dissociates (T 1/2 = 8--14 min). A more stable complex is found in acidic medium. Ceruloplasmin is one of the blood serum proteins able to interact with big gastrin. The stability of hormone-protein complex, formed by gastrin and ceruloplasmin, is dependent upon hormone concentration. With the addition of C-terminal penta--and octapeptides to labelled hormone, binding increased. It is speculated that formation of labile gastrin-blood protein complexes is necessary for selective gastrin transport from hormone-producing cells to target cells.

Animals

Pseudocholinesterase activity of human whole blood, bank blood, and blood protein solutions.

Pseudocholinesterase (E.C. 3.1.1.8) activity was measured in plasma of whole blood, bank blood, and several commercially available blood protein solutions by means of a colorimetric assay technique at 25 degrees C, pH 7.7, and with butyrylthiocholine as substrate (Merckotest-R No. 3337). Activity of whole blood was 5.79 plus or minus 0.20 U x ml-1, of bank blood 4.53 plus or minus 0.27 U x ml-1, and of two human serum solutions (Biseko-R, Seretin-R) 3.05 plus or minus 0.13 and 3.04 plus or minus 0.22 U x ml-1, respectively (mean plus or minus S.E.M.). The other blood protein solutions contained no clinically significant esterase activity. Since transfusion of blood plasma has been suggested for treatment of cholinesterase deficiency and postoperative suxamethonium-induced muscle paralysis, an in-vitro attempt was carried out to correlate the amount of plasma necessary and the rise of pseudocholinesterase activity in the recipient's blood: A large amount of blood has to be transfused to yield a comparatively small increase in esterase activity. Thus, considering the potential hazards of blood transfusion, this treatment does not seem to be advisable.

Anesthesia, General

Storage of proteins in the rough endoplasmic reticulum of human hepatocytes in a patient with normal blood proteins, on oral contraceptives.

Aspects of protein storage in the rough endoplasmic reticulum of hepatocytes, comparable with those reported in alpha1-antitrypsine (AAT) deficiency, have been observed in the course of jaundice in a woman presenting no evident abnormality in AAT or other blood proteins. In light microscopy, most hepatocytes contained characteristic globular inclusions but they were PAS negative and did not react with anti-AAT antibodies. This storage of protein ceased at the time the jaundice disappeared. Prolonged treatment with high doses of contraceptive steroids may have been involved in this peculiar reaction of the hepatocytes.

Adult

Profile analysis of blood proteins with a centrifugal analyzer.

We describe a procedure for routine analysis of a profile composed of eight blood proteins with a GEMSAEC centrifugal analyzer. The end-point technique is used and four standards are included in each run in the immunochemical analysis of the individual proteins. Additional computer programs fit the absorbance readings from the samples to the (nonlinear) standard curve and store the results in a patient's file for a final printout, which also presents the patient's data and reference values. The proteins are analyzed in a given order, which allows common blank runs to be used. Antisera are used in suitably high concentrations, so that the "antigen in excess" problem only appears for analysis of IgA and IgM when sera contain high amounts of the M-components of these two classes. The capacity, accuracy, and precision of the method are satisfactory.

Antigen-Antibody Reactions

[Effect of a 49-day space flight on immunological reactivity indices and on the blood protein makeup in the crew of Saliut-5].

The prolonged 49-day space flight resulted in a significant inhibition of immunological reactivity of the Salyut-5 crewmembers which involved a decline in bactericidal activity of the serum and lysozyme activity of the saliva, and a decrease in the content of immunoglobulins in the saliva and tonsillary lacunae. After the flight recovery of reduced immunoreactivity took a longer time than after shorter-term flights. The prolonged space mission led to an increase of most globulin fractions and a decrease of albumin in blood. With respect to globulin fractions, a predominant increase in the content of C3c and C4-factors of the complement and immunoglobulins G, A, M was noted. Blood proteins returned to normal within a long period of time.

Antigen-Antibody Reactions

Gene mutations (de novo) found in electrophoretic studies of blood protein of infants with anomalous development.

Twelve proteins of enzymic and nonenzymic nature in blood samples of infants that deviate from the average population in physical development (50 premature and 177 full-term infants with rough and multiple developmental defects) were studied by electrophoresis in polyacrylamide and starch gels. The control group consisted of 500 normal newborns. In infants with developmental disorders, the frequency of rare electrophoretic protein variants was found to be about one order of magnitude higher than in the control. It has been shown for at least five cases that such variants are de novo mutations. According to these data the mutation rate is approximately 2 x 10(-3) per locus per generation for the group selected and approximately 6 x 10(-5) for the total population. Despite the fact that further specification of the estimations found is required, we consider the results obtained as evidence in favor of the efficiency of the earlier substantiated monitoring model of gene mutations in the human population [Dubinin, N.P. & Altukhov, Yu. P. (1977) in Genetic Consequences of Environmental Pollution, ed. Dubinin, N.P. (Mysl, Moscow), pp. 14-45]. This approach, which infers electrophoretic screening of blood proteins in a specially selected group of newborns, makes it possible to reduce the size of samples needed for statistically reliable estimations of the alteration of mutation rate.

Blood Group Antigens