Publications
495 results found
Morris HR, Williams DH, Midwinter GG, et al., 1974, A mass-spectrometric sequence study of the enzyme ribitol dehydrogenase from Klebsiella aerogenes., Biochem J, Vol: 141, Pages: 701-713, ISSN: 0264-6021
The first detailed results of the application of a low-resolution mixture analysis approach to the sequence analysis of an enzyme, ribitol dehydrogenase, are given. Examples of the interpretation of the spectra of peptide mixtures derived from this protein are described. Evidence for new fragmentation patterns observed is reported, together with an explanation of the generation of ambiguous sequences by use of a low-specificity enzyme, thermolysin. The overall sequencing strategy evolved is assessed.
Bridgen J, Morris HR, 1974, Use of mass spectrometry and quantitative Edman degradation for the determination of repeating amino-acid sequences., Eur J Biochem, Vol: 44, Pages: 333-334, ISSN: 0014-2956
Morris HR, Batley KE, Harding NC, et al., 1974, Dihydrofolate reductase: low-resolution mass-spectrometric analysis of an elastase digest as a sequencing tool., Biochem J, Vol: 137, Pages: 409-411, ISSN: 0264-6021
An elastase digest of a protein of unknown structure, dihydrofolate reductase, was studied by mass spectrometry. This soluble digest contained a large number of small peptides in different yields, within the ideal molecular-weight range (200-1200) for mixture-analysis mass spectrometry. Sequences of the major component peptides in the digest are reported.
Morris HR, 1974, Peptide sequence determination by mass spectrometry, Biochemical Society Transactions, Vol: 2, Pages: 806-808, ISSN: 0300-5127
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- Citations: 6
DELL A, MORRIS HR, 1974, NEW OBSERVATIONS ON FRAGMENTATION PROPERTIES OF PEPTIDES UNDER ELECTRON-IMPACT MASS-SPECTROMETRY, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol: 61, Pages: 1125-1132, ISSN: 0006-291X
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- Citations: 8
MAGNUSSO S, SOTTRUPJ L, PETERSEN TE, et al., 1974, PRIMARY STRUCTURE OF VITAMIN-K-DEPENDENT PART OF PROTHROMBIN, FEBS LETTERS, Vol: 44, Pages: 189-193, ISSN: 0014-5793
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- Citations: 299
DELL A, MORRIS HR, WILLIAMS DH, et al., 1974, DETERMINATION OF SEQUENCE INFORMATION IN HOMOLOGOUSLY RELATED PROTEINS BY MASS-SPECTROMETRY, BIOMEDICAL MASS SPECTROMETRY, Vol: 1, Pages: 269-273, ISSN: 0306-042X
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- Citations: 8
Hunt E, Morris HR, 1973, Collagen cross-links. A mass-spectrometric and 1H- and 13C-nuclear-magnetic-resonance study., Biochem J, Vol: 135, Pages: 833-843, ISSN: 0264-6021
1. The structure of a tetrafunctional cross-link (compound C) isolated from borohydride-reduced cow skin collagen has been determined by the combined use of mass spectrometry and (1)H and (13)C n.m.r. spectroscopy. 2. A new technique, of potentially wide applicability, is described for the mass-spectrometric determination of functional groups. 3. Detailed study of protonation shifts in the (13)C spectrum has allowed an unambiguous assignment of the exact structural relationship of the component parts of the molecule. 4. New interpretations of existing data on this molecule are given.
Morris HR, Dickinson RJ, Williams DH, 1973, Studies towards the complete sequence determination of proteins by mass spectrometry: derivatisation of methionine, cysteine and arginine containing peptides., Biochem Biophys Res Commun, Vol: 51, Pages: 247-255, ISSN: 0006-291X
Morris HR, Williams DH, 1972, The identification of a mutant peptide of an abnormal haemoglobin by mass spectrometry, Journal of the Chemical Society, Chemical Communications, Vol: 0, Pages: 114-116, ISSN: 0022-4936
A mutant peptide from an abnormal haemoglobin, contaminated by a second peptide, has been sequenced by mass spectrometry; the spectrum of one derivatised mixture allowed the sequences Leu-Leu-Gly-Asn-Val-Leu-Phe and Leu-Leu-Val-Val-Tyr-Pro-Trp to be determined.
Morris HR, 1972, Studies towards the complete sequence determination of proteins by mass spectrometry; a rapid procedure for the successful permethylation of histidine containing peptides., FEBS Lett, Vol: 22, Pages: 257-260
Morris HR, Williams DH, Ambler RP, 1971, Determination of the sequences of protein-derived peptides and peptide mixtures by mass spectrometry., Biochem J, Vol: 125, Pages: 189-201, ISSN: 0264-6021
Micro-quantities of protein-derived peptides have been converted into N-acetylated permethyl derivatives, and their sequences determined by low-resolution mass spectrometry without prior knowledge of their amino acid compositions or lengths. A new strategy is suggested for the mass spectrometric sequencing of oligopeptides or proteins, involving gel filtration of protein hydrolysates and subsequent sequence analysis of peptide mixtures. Finally, results are given that demonstrate for the first time the use of mass spectrometry for the analysis of a protein-derived peptide mixture, again without prior knowledge of the protein or components within the mixture.
Lawson DE, Fraser DR, Kodicek E, et al., 1971, Identification of 1,25-dihydroxycholecalciferol, a new kidney hormone controlling calcium metabolism., Nature, Vol: 230, Pages: 228-230, ISSN: 0028-0836
Lucas F, Barber M, Wolstenholme WA, et al., 1969, Mass-spectrometric determination of the amino acid sequences in peptides isolated from the protein silk fibroin of Bombyx mori., Biochem J, Vol: 114, Pages: 695-702, ISSN: 0264-6021
Several peptides were isolated from the protein silk fibroin of Bombyx mori by means of ion-exchange chromatography of a chymotryptic digest. The sequences of three of the peptides, Gly-Ala-Gly-Tyr, Gly-Val-Gly-Tyr and Gly-Ala-Gly-Ala-Gly-Ala-Gly-Tyr, were known from previous chemical work, but the sequence of the fourth, Gly-Ala-Gly-Val-Gly-Ala-Gly-Tyr, was previously only partially known. The necessary volatility for mass-spectrometric examination of the peptides was achieved by permethylation of the N-acetyl-peptide methyl ester derivatives. From the mass spectra it was possible to confirm the known sequences and to establish that of the partially known one. In one instance it was possible to deduce from the same mass spectrum the sequence of a main peptide component and that of a small amount of contaminating peptide. These results demonstrate for the first time the use of mass spectrometry in the determination of the amino acid sequences in peptides from a protein hydrolysate.
Morris HR, Geddes AJ, Graham GN, 1969, Some problems associated with the amino acid-sequence analysis of proteins by mass spectrometry., Biochem J, Vol: 111, ISSN: 0264-6021
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