Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 95 (1973), S. 880-886 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 12 (1973), S. 3387-3394 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 16 (1977), S. 3514-3518 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    ISSN: 1369-1600
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract Opioids, reported originally to bind to specific receptors in the brain, now also appear to bind to receptors on blood cells. The high prevalence of anemia among chronic opioid users leads us to propose that chronic opiate use results in elevated mu opioid receptor levels on human erythrocytes and that these receptor changes may affect erythrocyte membrane properties. Blood samples from 17 opioid-dependent subjects (based on the Diagnostic and Statistical Manual of Mental Disorders, 4th edition or DSM-IV) and 15 drug-free controls were assayed for mu opioid receptors on erythrocytes using a flow cytometry immunoassay. Deformability and the hydration status of erythrocytes were studied by ektacytometry. Data were analyzed by independent t-tests, tests of correlation, chi square and cluster analyses. As expected, the percentage of erythrocytes from opioiddependent subjects with opioid receptors (opioid receptor levels) was significantly higher (47.4 ± 38.3%) than controls (22.8 ± 30.1%) (t = 2.01, df = 30, p 〈 0.05). Also, the opioid-dependent patients showed a wide variation in the percentage of erythrocytes bearing opioid receptors and data analyses of these patients showed two strongly defined clusters. One subgroup consisted of nine individuals with very high receptor levels (mean = 81.5%) while the other had eight patients with low receptor levels (mean = 9.1%) that were not significantly different than the receptor levels of controls. Ektacytometry of opioid dependent patients with high opioid receptor levels showed changes in rheological parameters of erythrocytes, such as deformability index and cellular hydration. For example, a positive correlation was observed between opioid receptor levels and deformability indices among opioid-dependent patients (r = 0.74, p 〈 0.005). Our findings indicate that the mu opioid receptor is present on human erythrocytes, although with considerable variation in receptor levels, and that the levels of this receptor are significantly elevated with chronic opioid exposure. Moreover, erythrocytes with high opioid receptor levels from chronic opiate users seem to have high deformability. This study may offer clues to the biological properties of peripheral blood cells that may be mediated by mu opioid receptors and lead to a better understanding of some of the clinical effects of opioid use.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Immunogenetics 9 (1979), S. 183-192 
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A series of known sequential polypeptides is being synthesized and used in our laboratory to study the contribution of antigen structure, i. e., amino acid sequence and conformation in antigen recognition and specificity of the immune response. The capacity to respond to one such α-helical polypeptide (T-G-A-Gly)n, is T-cell dependent and restricted to mice of theH- 2b haplotype. The response is controlled by anIr gene mapping to theK region and/or theIA subregion which allows the animal to make both a T-cell mediated response, as well as a humoral response to the polypeptide. The response of three mutant strains at theK end of the major histocompatibility locus (MHC) need not differ from that of the responder parental haplotype. PETLES obtained from mice possessing a responder haplotype proliferate when cultured in vitro with (T-G-A-Gly)n. The antibody level of individual inbred mice of a given strain at a given time differs significantly (from 80% binding to less than 10% antigen bound in 3 out of 57 mice). There is also great individual variability in time of appearance of the antibody response and where peak optimal levels are seen. Possible explanations for the variation in the antibody expression include: (a) the polymer is a weak immunogen, (b) the presence of modifier gene(s) outside of the major histocompatibility complex controlling the magnitude of the antibody level, (c) the possible effect of the polymer which is a B cell mitogen as a generator of suppressor T cells and, (d) a feedback mechanism effect on B cells controlling the antibody level.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 6
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Immune responses to the sequential helical polypeptide (Tyr-Ala-Glu-Gly)n [(T-A-G-Gly)n] in mice is under the control of at least two separate genes. One gene,Ir-(T-A-G-Gly)-1, which is linked, toH-2 haplotypesb, f, andr, controls the ability to respond and maps to theIA subregion. A non-H-2-linked locus,Ir-(T-A-G-Gly)-2. is responsible for the magnitude of the antibody response, which is expressed as a high, intermediate, or low level of antibody production. The antibody produced is of the IgG class, and does not crossreact even with the closely related sequential helical polymer (Tyr-Glu-Ala-Gly)n [(T-G-A-Gly)n]. Immune responsiveness is a dominant trait,i.e., the F1 generations of responder x nonresponder crosses are responders. However, the data obtained with both backcross populations are not easily interpretable. The contribution of the B-cell mitogenic activity of the sequential polymer to activation of suppressor T cells is considered as a possible explanation for the backcross results. The possible role of the Ia. W29 specificity present in the mouse strains responding to both (T-A-G-Gly)n and calf skin collagen type I in modulating responses to the polymers is discussed.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 7
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Six sequential polytetrapeptides containing equimolar amounts of tyrosine, glutamic acid, alanine, and glycine were characterized by CD and difference spectroscopy over a wide range of pH. As the pH was lowered from physiological values, each of the polymers underwent pH-sensitive transitions. The CD spectra indicated that two polymers, poly(Tyr-Glu-Ala-Gly) and poly(Tyr-Ala-Glu-Gly), had some α-helical conformation at pH 7.0 and approached maximum helicity around pH 6.0; two others, poly(Ala-Tyr-Glu-Gly) and poly(Glu-Ala-Tyr-Gly), had no α-helical conformation at pH 7.0 and about one-third of the ellipticities of the above two polymers at pH 5.5; and the remaining two, poly(Ala-Glu-Tyr-Gly) and poly(Glu-Tyr-Ala-Gly) had little or no α-helix, even at pH 5.5. Difference spectroscopy at 286 nm yielded results quite different. The molar extinction coefficients for poly(Tyr-Glu-Ala-Gly) and poly(Tyr-Ala-Glu-Gly) continued to change, even below pH 5.5, and the total changes in absorbance between pH 8.0 and 4.5 were of intermediate magnitudes among the six polymers. Poly(Ala-Tyr-Glu-Gly) and poly(Glu-Ala-Tyr-Gly), which had similar CD spectra, had the lowest and highest pH-related changes in the molar extinction coefficients. It thus appears that amino acid composition alone cannot account for the apparent differences in conformation among the polytetrapeptides. Other factors, such as amno acid sequence, must play a major role in the determination of conformation.The intrinsic viscosity of poly(Tyr-Glu-Ala-Gly) increased markedly between pH 6.0 and 5.5, which was below the pH of the CD transition but above the pH at which the largest absorption perturbation change, at 286 nm, took place. The model that can best account for the relatively low pH at which the absorption transition of tyrosine occurred is a progressive immobilization of side chains in the α-helix as the pH decreases.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 8
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The monomers γ-benzylglutamyl-ε-benzyloxycarbonyl-lysylalanylglycine pentachlorophenyl ester and alanyl-γ-benzyl-D-glutamyl-ε-benzyloxycarbonyllysyl-D-alanyl-glycine pentachlorophenyl ester, were polymerized in dilute solutions of dimethylform-amide (DMF) or as dispersions in the same volume of benzene. After deprotection with hydrogen bromide, the products were either chromatographed on Sephadex G-50 or dialyzed. The polymers derived from the polymerization in benzene were considerably larger than those from DMF. The results in benzene indicated that high monomer to solvent ratios are not necessary for the production of high-molecular-weight sequential polypeptides. Circular dichroism spectra of the polymers and monomers at neutral and acid pH indicated that poly(L-Glu-L-Lys-L-Ala-Gly) exists in a random coil configuration and poly(L-Ala-D-Glu-L-Lys-D-Ala-Gly) exists in a β conformation.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 9
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Two sequential polypeptides, poly(O-benzyl-L-Tyr-γ-benzyl-L-Glu-L-Ala-Gly) and poly(ε-benzyloxycarbonyl-L-Lys-L-Glu-L-Ala), were synthesized, the former by the pentachlorophenyl ester of the tetrapeptide monomer and the latter by the azide of the tripeptide monomer. After deprotection and dialysis, poly(L-Tyr-L-Glu-L-Ala-Gly) was obtained in 71% yield and had a molecular weight of 53,000. The circular dichroism spectra (CD) of the polymer at pH's 7.2, 10.5, and 11.8 and of oligomers and of the monomer at pH 7.2 indicated that the polymer exists in an α-helical conformation.After deprotection, poly(L-Lys-L-Glu-L-Ala) was obtained in 37% yield and had a molecular weight of 3000. The CD spectra of the polymer at pH 7.2 and 2.8, and of the monomer at pH 7.2, indicated that the polymer is in a randomly coiled configuration.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...