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201.
Giampaolo Venditti Elisabetta Schievano Luciano Navarini Stefano Mammi 《Food biophysics》2011,6(2):321-326
Water distribution in green coffee was studied by means of pulsed nuclear magnetic resonance (NMR). Hydration experiments for relaxometry measurements were performed by adding either H2O or D2O to dried green coffee beans up to 35% (dry basis) or, alternatively, by moisture absorption in a controlled humidity environment. The CPMG experimental relaxation decay curves were acquired using a benchtop time-domain NMR analyzer at each hydration level and as a function of time. All NMR data were fitted according to the Laplace inversion approach to obtain the proton mobility distributions of water in the hydrated beans. By comparing the T 2 relaxograms of the hydrated beans with the ones observed in the untreated raw beans, it was found that up to ??10% water exhibits a rather restricted proton mobility. Hydration experiments carried out with D2O highlighted the contribution of the chemical exchange between the water protons and those of the solid matrix to the overall NMR signal. A possible interpretation of the data in terms of the antiplasticizer and plasticizer effect of water is offered. 相似文献
202.
Giampaolo Manao Luigia Pazzagli Paolo Cirri Anna Caselli Guido Camici Gianni Cappugi Ahmad Saeed Giampietro Ramponi 《The protein journal》1992,11(3):333-345
Two lowM r phosphotyrosine protein phosphatases have been isolated from rat liver. The enzymes were previously known as lowM r acid phosphatases, but several recent studies have demonstrated that this family of enzymes possesses specific phosphotyrosine protein phosphatase activity. We determined the complete amino acid sequences of the two isoenzymes and named them AcP1 and AcP2. Both consist of 157 amino acid residues, are acetylated at the NH2-terminus, and have His as the COOH-terminus. The molecular weights calculated from the sequences are 18,062 for AcP1 and 17,848 for AcP2. They are homologous except in the 40–73 zone, where about 50% of residues are different. This fact suggests that the two isoenzymes are produced by an alternative splicing mechanism. There is no homology between these two isoenzymes and the receptor-like phosphotyrosine protein phosphatases LAR, CD45, human placenta PTPase 1B, and rat brain PTPase-1. AcP1 and AcP2 are also distinct from rat liver PTPase-1 and PTPase-2, since these last enzymes have higher molecular weights. AcP1 differs from AcP2 with respect to (1) substrate affinity and (2) its sensitivity to activators and inhibitors, thus suggesting a their different physiological function. 相似文献
203.
The possibili that urinary glutamine transaminase K activity might be a marker of a proximal tubule segment-specific response to mercuric chloride was investigated in male rats after a single i.p. injection in time-course and dose-response experiments. Urinary total proteins and angiotensin converting enzyme activity were determined simultaneously. Urinary indices showed an early increase (within 5 h of treatment) of total proteins and angiotensin converting enzyme, whereas glubmine transaminase K increased 10 h after treatment. The peak of all these indices was observed 24 h after mercuric chloride injection. The lowest dose that induced a significant increase in proteins and enzymes was 0.25 mg kg-1; in addition, a dose-response effect was observed. Glutamine transaminase K appeared to be an early and sensitive index of response of mercuric chloride effects, similar to total proteins and angiotensin converting enzyme. It is suggested that this enzyme is mainly localized in the 'pars recta' of the proximal tubule. Therefore glutamine transaminase K might be a segment-specific marker for the detection of damage localized in this portion of the proximal tubule. 相似文献
204.
Massimo Stefani Alessandra Modesti Guido Camici Giampaolo Manao Gianni Cappugi Andrea Berti Giampietro Ramponi 《Journal of Protein Chemistry》1986,5(5):307-321
The complete amino acid sequence of duck skeletal muscle acylphosphatase is presented. The sequence was studied by the manual Edman degradation of the complete series of tryptic peptides and the amino acid composition of peptic peptides. The NH2-terminus is acetylated, and the polypeptide consists of 102 amino acid residues. The sequence is compared with other known acylphosphatases from the skeletal muscle of several vertebrate species. 相似文献