Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0393754 (HSA)
 2,996 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

CKS-17, an immunosuppressive peptide homologous to certain retroviral transmembrane envelope protein, has been shown to inhibit lymphocyte proliferation in response to mitogens or alloantigens when covalently attached to bovine serum albumin (CKS-17-BSA). To define its site of action, we determined if CKS-17 conjugated to human serum albumin (CKS-17-HSA) could block the direct activation of lymphocytes by phorbol-12-myristate-13-acetate (PMA) or by a synthetic diacylglycerol, dioctanoylglycerol (DiC8). CKS-17-HSA inhibited lymphocyte proliferation in response to PMA and ionomycin in a dose-dependent manner with up to 88% inhibition occurring with 15 microM CKS-17-HSA. The conjugated peptide also inhibited the proliferation of lymphocytes in response to DiC8 and ionomycin by up to 57% at 15 microM CKS-17-HSA. Based on these findings we investigated the effect of CKS-17-HSA on the activity of protein kinase C (PKC), an enzyme directly activated by PMA and DiC8. PKC was isolated chromatographically from the cytosol of human neutrophils or the human lymphoblastoid cell line Jurkat. CKS-17-HSA caused a dose-dependent enzyme inhibition with a concentration giving half-maximal inhibition (IC50) of ca.3 microM and greater than 95% inhibition at 15 microM CKS-17-HSA. Inhibition of PKC by the conjugated peptide was not reversed by increasing concentrations of Ca2+, Mg2+, phosphatidylserine, diolein, or adenosine triphosphate (ATP), indicating that the conjugated peptide did not function as a chelator or competitive inhibitor. In contrast to its effects on PKC, CKS-17-HSA did not inhibit the activity of adenosine 3':5'-cyclic monophosphate (cyclic AMP)-dependent protein kinase (PK-A) nor the calcium and phospholipid-independent form of PKC (PK-M). Moreover the peptide inhibited in vivo PKC activity in cytosol of intact cells and in membrane of PMA-stimulated cells. These results suggest that the inhibition of lymphocyte proliferation by CKS-17-HSA may be due to the direct inactivation of PKC.
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PMID:A synthetic peptide homologous to retroviral transmembrane envelope proteins depresses protein kinase C mediated lymphocyte proliferation and directly inactivated protein kinase C: a potential mechanism for immunosuppression. 192 61

In the pH 7.2 Na2HPO4-NaH2PO4 buffer solutions and in the presence of PEG-6000, fenvalerate (Fen) antisera was combined with Fen specifically, and aggregated to form immune complex particles that exhibited five resonance scattering peaks at 350, 390, 420, 440 and 480 nm respectively. The peak at 390 nm was the strongest and was chosen for use. Fen concentration (c) in the range of 0.20 to 6.40 microg x mL(-1) was proportional to the resonance scattering intensity at 390 nm. Its regression equation was DeltaIRS 23.05c-1.39, the correlation coefficient was 0.9978, and the detection limit was 0.07 microg x mL(-1). Effects of buffer solution type, pH value, buffer solution volume, fenvalerate antisera concentration, PEG-6000 concentration, incubation temperature and time on the resonance scattering intensity were considered in detail. With pH (5.8-8.0) increasing, the IRS and Ib all decreased. When the pH value was at 7.2, the DeltaIRS was bigger. Three buffer solutions of pH 7.2, including Na2HPO4-citric acid, Na2HPO4-KH2PO4 and Na2HPO4-NaH2PO4, were examined. The pH 7.2 Na2HPO4-NaH2PO4 buffer solution gives the biggest DeltaIRS value. PEG-6000 could enhance the DeltaIRS value. When the concentration of PEG-6000 was 50.0 mg x mL(-1), the DeltaIRS was achieved at max. Fen was a stable chemical. The IRS increased within 20 min,while the DeltaIRS remained constant when incubation time was in the range of 20-40 min. The condition of a pH 7.2 Na2HPO4-NaH2PO4 buffer solution-50.0 mg x mL(-1) PEG-6000-6.67 microg x mL(-1) Fen antisera-30 degrees C-incubation time 20 min was chosen. According to the procedure, the influence of foreign substances on the determination of 1.60 microg x mL(-1) Fen was examined, within a relative error of +/- 5%. Results showed that the following coexistent substances had no impact on the RS assay: 96 microg x mL(-1) ametryne, 96 microg x mL(-1) m-aminotoluene, 48 microg x mL(-1) simetryne, 48 microg x mL(-1) p-aminotoluene,80 microg x mL(-1) BSA, 80 microg x mL(-1) HSA, 80 microg x mL(-1) Fe3+, 80 microg x mL(-1) Mg2+, 160 microg x mL(-1) Ca2+, and 160 microg x mL(-1) glucose. The results indicated that this RSS assay has good selectivity. This immune resonance scattering spectral assay was applied to the determination of Fen in waste water samples with satisfactory results. The recovery was in the range of 92.91%-101.25%, and the relative standard deviation was in the range of 1.71%-4.80%.
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PMID:[Immune resonance scattering spectral analysis of fenvalerate]. 1938 42

Using tri-sodium citrate as reducer, stable silver nanoparticles the size of about 20 nm were prepared by the microwave high pressure procedure with simplicity and rapidity. At pH 9.0, sliver nanoparticle was used to label goat anti-human IgG (GIgG) to obtain an immuno-nanosilver resonance scattering spectral probe (AgGIgG) for IgG. In pH 6.0 buffer solution and in the presence of polythylene glycol (PEG) and KCl, the immune reaction of IgG with AgGIgG took place, the silver nanoparticles released from AgGIgG produced aggregations, and the resonance scattering intensity at 485 nm (I(485 nm)) was enhanced greatly. The influence factors such as pH value, buffer solution volume, concentration of AgGIgG, KCl, PEG-4000, PEG-6000, PEG-10000 and PEG-20000, incubation temperature and time were considered, respectively. Under the conditions of 0.40 mL of pH 6.0 phosphate buffer solution, 1.20 mL of 9.8 microg x mL(-1) AgGIgG, 0.20 mL of 20% PEG-6000, 0.50 mL of 10% KCl, and ultrasonic irradiation for 25 min at room temperature, the increased intensity deltaI(485 nm), was proportional to the IgG concentration (c(IgG)) from 0.004 to 0.48 microg x mL(-1), with a detection limit of 2.4 ng x mL(-1). The regress equation was deltaI485 nm = 76.8c(IgG) + 4.7. The effect of foreign substances such as 20 microg x mL(-1) Ni2+, Fe2+, Pb2+ and BSA,60 microg x mL(-1) Cu2+, Ca2+ and HSA,60 microg x mL(-1) Mg2+ and Mn2+, 320 microg x mL(-1) Zn2+, glucose and urea on the deltaI(485 nm) was examined, respectively. Results showed that there was no interference. This assay showed high sensitivity and good selectivity for quantitative determination of IgG in human serum with satisfactory results. The analytical results were in agreement with that of the reference results.
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PMID:[A new immuno-nanosliver resonance scattering spectral probe for assay of IgG]. 1981 May 49

In acetate buffer solution and in the presence of glucose oxidase (GOD), glucose reduced the dissolved oxygen to form H2O2 that oxidized catalytically the excess KI to from I3- by horseradish peroxidase (HRP). The I3- combines respectively with rhodamine S (RhS), rhodamine 6G(Rh6G), butyl-rhodamine B(b-RhB) and rhodamine B(RhB) to form RhS-I3, Rh6G-I3, b-RhB-I3 and RhB-I3 associated particles that result in fluorescence quenching at 556, 556, 584 and 584 nm, respectively. Under the optimal conditions, the concentration of glucose in the range of 0.083-9.99, 0.17-8.33, 0.33-8.33 and 0.33-9.99 micromol x L(-1) is linear with their fluorescence quenching at 556, 556, 584 and 584 nm, with detection limits of 0.059, 0.17, 0.21 and 0.16 micromol x L(-1) glucose. And the regression equation was deltaF = 40.0c + 3.0, deltaF = 23.9c + 8.1, deltaF = 25.6c + 4.2, and deltaAF = 18.4c + 0.8, respectively. The RhS system was the most sensitive and stable, and was chosen for use. Influence of some foreign substances on the RhS fluorescence quenching determination of 6.67 micromol x L(-1) glucose was examined, with a relative error of +/- 10%. Results showed that 1000-fold Mg2+ and Cu2+, 300-fold Mn2+, 100-fold Zn2+, Al3+ and Co2+, 60-fold L-tyrosine, urea and nicotinic acid, 50-fold Fe3+, HSA and BSA, 10-fold sucrose, vitamin B2, L-lysine, L-glutamic acid and L-cystine did not interfere with the determination. This RhS fluorescence quenching assay was applied to the determination of glucose in the serum samples with satisfactory results.
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PMID:[Fluorescence analysis of trace glucose using glucose oxidase and horseradish peroxidase]. 1995 Jun 69