Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rabbit antisera prepared against conjugates of the benzylpenicilloyl (BPO) bifunctional haptenic group were analyzed to determine whether the antibodies are adapted to only a portion of the large BPO molecule, or to the entire molecule, and whether specificity extends to the lysine side chain and adjoining structures of the immunizing carrier protein. No antibodies adapted to the phenylacetylamine portion of the BPO group could be detected in a pooled rabbit anti-BPO serum globulin fraction by PCA and quantitative precipitin analysis using several phenylacetylamine-protein conjugates as antigens. No antibodies adapted only to the thiazolidine carboxylic acid portion of the BPO molecule were detected in the anti-BPO globulin fraction using quantitative precipitin and hapten inhibition methods. At least the bulk of the anti-BPO antibodies was found to be adapted to the entire BPO haptenic group. By quantitative hapten inhibition of precipitation of the anti-BPO globulin fraction, the anti-BPO antibodies were found to show specificity for a 6 carbon amide side chain corresponding to the lysine side chain through which BPO groups are bound predominantly to protein. The contribution of this 6 carbon chain to antibody-hapten binding was small; (-DeltaF degrees ) was calculated to be 460 calories per mole (average). Rabbit anti-BPO antibodies prepared against BPO-rabbit serum albumin conjugates showed specificity also toward structures of the immunizing carrier protein, and possibly toward secondary or tertiary structural configurations. Penicilloyl conjugates of rabbit serum albumin precipitated from 3 individual rabbit antisera more anti-BPO antibodies than did penicilloyl conjugates of heterologous carriers (poly-L-lysine, human serum albumin, and human gamma-globulin). Anti-BPO antibodies demonstrated heterogeneity with regard to closeness of fit to the haptenic group, or with regard to the dimensions of the combining sites, or both. It was concluded that at least a large part of anti-BPO antibodies are specifically adapted to a large antigenic unit comprised of the entire BPO group, the lysine side chain, and structural configurations of the immunizing carrier protein.
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PMID:Studies on the dimensions of the rabbit antibenzylpenicilloyl antibody-combing sites. 1393 Jan 42

A critical comparison of the various PCA methods on the absorbance matrix data concerning the complexation equilibria between SNAZOXS and Cd(2+), Co(2+), Cu(2+), Ni(2+), Pb(2+) and Zn(2+) or Naphtylazoxine 6S and Cd(2+), Cu(2+), Ni(2+) and Zn(2+) at 25 degrees C is performed. The number of complex species in a complex-forming equilibria mixture is the first important step for further qualitative and quantitative analysis in all forms of spectral data treatment. Therefore, the accuracy of the nine selected index functions for the prediction of the number of light-absorbing components that contribute to a set of spectra is critically tested using the principal component PCA algorithm INDICES in S-Plus software. Four precise methods based upon a knowledge of the experimental error of the absorbance data and five approximate methods requiring no such knowledge are discussed. Precise methods always predict the correct number of components even a presence of the minor species in mixture. Due to the large variations in the index values and even at logarithmic scale they do not reach an obvious point where the slope changes. An improved identification with the second or third derivative and derivative ratio function for some indices is preferred. Behind the number of various complexes formed the stability constants of species ML, ML(2), (and ML(3), respectively) type logbeta(11), logbeta(12), (and logbeta(13), respectively) for the system of SNAZOXS (ligand L) with six metals (the standard deviation s(logbeta(pq)) of the last valid digits are in brackets) Cd(2+) (4.50(3), 8.36(7)), Co(2+) (5.75(6), 9.79(9), 13.05(2)), Cu(2+) (6.69(6), 11.40(7)), Ni(2+) (6.44(8), 10.91(11), 15.07(10)), Pb(2+) (5.63(5), 9.97(9)) and Zn(2+) (5.11(3), 8.84(5)) and for system of Naphtylazoxine 6S with Cd(2+) (6.08(4), 11.44(7), 16.06(11)), Cu(2+) (7.80(8), 13.41(14)), Ni(2+) (6.35(12), 11.43(19), 16.68(24)) and Zn(2+) (7.01(8), 12.65(15)) at 25 degrees C are estimated with SQUAD(84) nonlinear regression of the mole-ratio spectrophotometric data. The proposed strategy of an efficient experimentation in a stability constants determination, followed by a computational strategy, is presented with goodness-of-fit tests and various regression diagnostics able to prove the reliability of the chemical model proposed.
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PMID:Number of species in complexation equilibria of SNAZOXS or Naphtylazoxine 6S and Cd(2+), Co(2+), Cu(2+), Ni(2+), Pb(2+) and Zn(2+) ions by PCA of UV-vis spectra. 1897 20

Pterygium, a common ophthalmic disease that is caused by fibrovascular growth of conjunctiva and conjunctival melanocytic nevi that is another conjunctival disease, are detected by Raman spectroscopy in the present study. We find that there is an obvious increase in the intensity at the peak of 1,583 cm(-1) that is assigned to C=C unsaturated fatty acids stretch of lipids in the pterygium tissue, and 1,639 cm(-1) also increased which belongs to amide I. Also, PCA (Principal Component Analysis) was used to classify the normal conjunctiva from the pterygium tissue. For the conjunctival melanocytic nevi, the intensity of Raman spectrum region between 1,550 cm(-1) and 1,650 cm(-1) that belong to protein has increased, which indicates that the content of protein in conjunctival melanocytic nevi is more richer than the normal ones.
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PMID:Micro-Raman spectroscopy study of human pterygium and conjunctival melanocytic nevi. 2254 93