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pro vyhledávání: '"James J. L'Italien"'
Autor:
James J. L'Italien
This volume surveys the current status of many of the important methods and approaches which are central to the study of protein structure and function. Many of the articles in this volume are written to emphasize the general utility of the method or
Autor:
James E. Strickler, James J. L’Italien
Publikováno v:
Analytical Biochemistry. 127:198-212
Peptide purification via high-performance liquid chromatography (HPLC) and solid-phase sequencing were integrated to form a system allowing the determination of complete sequence information on a microscale without the use of radiolabels or modified
Autor:
James J. L'italien, Stephen B. H. Kent
Publikováno v:
Journal of Chromatography A. 283:149-156
A novel class of isothiocyanates has been introduced for protein microsequencing. These modified phenylisothiocyanates (PITC) are substituted in the 4-position of the phenyl ring with a protected amine and have a general structure tert. -Boc-NH-(CH 2
Autor:
Flora Chow, Gary Opperman, Pamela Baker, Gary Long, James J. L'Italien, Susan M. Peterson, William Hays, Tomas Kempe, Brad Paulson
Publikováno v:
Nature Biotechnology. 4:565-568
A growth hormone releasing factor analog [Leu27,Hse44]GRF(1–44)lactone has been made by recombinant DNA techniques. The peptide was expressed from a multiple–copied GRF gene fused to lacZ. The monomeric GRF peptide analog with a C–terminal homo
Publikováno v:
Biochemistry. 20:5437-5443
Crambin, a hydrophobic plant seed protein, consists of a single chain of 46 amino acids with a calculated molecular weight of 4720. The primary structure was determined by using solid-phase sequencing techniques and was confirmed through X-ray crysta
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 702:117-124
A hydrophobic, chloroform-soluble tryptic peptide with a molecular weight of approximately 4000 has been purified from the bovine white matter proteolipid protein. Its primary structure was obtained by a combination of solid-phase Edman degradation a
Autor:
James J. L'italien, Richard A. Laursen
Publikováno v:
FEBS Letters. (2):359-362
Autor:
James J. L’Italien, Richard A. Laursen
Publikováno v:
Methods in Protein Sequence Analysis ISBN: 9781461258346
The rate determining step in the total sequence analysis of proteins, by protein chemical means, is generally found to be the isolation of purified fragments in sufficient quantity for sequence analysis. The amount of material necessary for automated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::811275cda8adf364dc744df0cb78bd40
https://doi.org/10.1007/978-1-4612-5832-2_32
https://doi.org/10.1007/978-1-4612-5832-2_32
Autor:
James J. L’Italien
Publikováno v:
Proteins ISBN: 9781461290018
Recent advances in the micropurification of polypeptides for structural analysis have centered upon individual improvements in the areas of HPLC (microbore), electrophoresis (electroblot) and bioaffinity chromatography (monoclonal antibody-immunoaffi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6acf6fd567ecea88ebb4e9e3e6ea3fd6
https://doi.org/10.1007/978-1-4613-1787-6_10
https://doi.org/10.1007/978-1-4613-1787-6_10
Autor:
James E. Strickler, James J. L’Italien
Peptide purification via high-performance liquid chromatography (HPLC) and solid-phase sequencing were integrated to form a system allowing the determination of complete sequence information on a microscale without the use of radiolabels or modified
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::89f5fc2cf73bb3c9b2b3b6a3915549e0
https://doi.org/10.1016/b978-0-12-335780-9.50028-0
https://doi.org/10.1016/b978-0-12-335780-9.50028-0