and Jörnvall, H., 1988 Class III human liver alcohol dehydrogenase. Kaiser, R., Holmquist, B., Hempel, J., Vallee, B.L. The primary structure of the protein chain of the ethanol-active isoenzyme, Eur. Jörnvall, H., 1970 Horse liver alcohol dehydrogenase. and Sletten, K., 1995 Purification and characterization of amyloid-related transthyretin associated with familial amyloidotic cardiomyopathy, Eur. Hermansen, L.F., Bergman, T., Jörnvall, H., Husby, G., Rankly, I. and Bergman, T., 1995 Analytical approaches to alcohol dehydrogenase structures, in: Enzymology and Molecular Biology of Carbonyl Metabolism 5, Weiner, H., Holmes, R.S., and Wermuth, B., eds., Plenum Press, New York, pp 417–426. Gheorghe, M.T., Lindh, I., Griffiths, W.J., Sjövall, J. Characterization, molecular cloning, and evolutionary implications on substrate specificity in the carboxypeptidase gene family, J. and Rutter, W.J., 1988 Anovel rat carboxypeptidase, CPA2. Gardell, S.J., Craik, C.S., Clauser, E., Goldsmith, E.J., Stewart, C.-B., Graf, M. and Pigon, A., 1991 Analysis of the structural relationship between the DNA-binding phosphoproteins pp42, pp43 and pp44 by in situ peptide mapping, Molecular Biology Reports 15: 65. 283: 100.īergman, T., 1994 Internal amino acid sequences via in situ cyanogen bromide cleavage, J. and Jörnvall, H., 1991 Direct analysis of peptides and amino acids from capillary electrophoresis, FEBS Lett. ![]() and Jörnvall, H., 1987 Electroblotting of individual polypeptides from SDS/polyacrylamide gels for direct sequence analysis, Eur. ![]() This process is experimental and the keywords may be updated as the learning algorithm improves.īergman, T. These keywords were added by machine and not by the authors. The protocol has been applied to both a synthetic peptide corresponding to the N-terminal segment of horse liver alcohol dehydrogenase and to the intact protein. In this manner, drawbacks as high protein consumption, long handling times and inaccessibility of the N-terminal fragment to Edman degradation, are avoided. proteolytic cleavage, HPLC of fragments and internal sequence analysis) we have tested direct chemical deacetylation using a mixture of trifluoroacetic acid and methanol (Gheorghe et al., 1995). ![]() To circumvent the conventional approach to sequence analysis of blocked proteins (i.e. Acetylation represents the most frequent N-terminal modification and is found in alcohol dehydrogenases among many other proteins. Tsunasawa and Hirano, 1993), but they often suffer from poor yields and a large extent of undesirable peptide bond cleavage. Several enzymatic and chemical methods to remove the blocking group have been suggested (cf. Frequently the modification involves an acetyl-, formyl- or pyroglutamyl-moiety coupled to the α-amino group and direct sequence analysis by Edman degradation is not possible. Proteins with a blocked N-terminus are common.
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