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  • 1
    Electronic Resource
    Electronic Resource
    Linked scans of peptides and protein digests: Amino acid sequence determination of components of complex mixtures (1989)
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 3 (1989), S. 110-116 
    Details
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: Two-sector linked-scan analysis of an unpurified proteolytic digest of a pyruvate decarboxylase enzyme (60 000 Da) has allowed the discovery and assignment of an amino-terminal post-translational modification and processing event. A difference in amino acid sequence from that predicted by a recently published nucleotide sequence has also been found. These results illustrate both the use and considerable potential of linked-scan methods for the analysis of complex biopolymer mixtures.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/rcm.1290030406
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  • 2
    Electronic Resource
    Electronic Resource
    Extended performance using a high field magnet mass spectrometer (1981)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 8 (1981), S. 463-473 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The development of a high field magnet for high mass electron impact, chemical ionization, field desorption and fast atom bombardment mass spectrometric studies is described. Its utility is illustrated with examples from structural studies of vitamin B12 biosynthetic intermediates, oligosaccharides, glycopeptides and the bleomycin antibiotics. The technique has also greatly assisted sequence studies of protein derived peptides.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200080920
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  • 3
    Electronic Resource
    Electronic Resource
    Primary structure of a chloramphenicol acetyltransferase: Mass spectrometric studies (1981)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 8 (1981), S. 128-136 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Low resolution electron impact mass spectrometry has been used as a major tool in the sequencing of a chloramphenicol acetyltransferase (mol. wt 25 668). Mass spectrometric data from mixtures of peptides from elastase, chymotryptic and subtilisin digests have defined 83% of the protein sequence. Several, previously unrecognized, peptide fragmentation pathways are reported.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200080310
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  • 4
    Electronic Resource
    Electronic Resource
    The determination of sequence information in homologously related proteins by mass spectrometry (1974)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 1 (1974), S. 269-273 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: An azurin, a small respiratory copper protein from the bacterium Pseudomonas fluorescens biotype G, has been studied by mass spectrometry to determine sequence information. The study of homologously related proteins by mass spectiometry is particularly attractive, since the correct nature of major parts of the deduced sequences can be confirmed by comparison with the sequences of the protein from related organisms. An oxidized tryptohan residue has been identified amongst the products from a cyanogen bromide digest of this wild type azurin. In the same digest, a product is also found to arise from cleavage of the peptide chain at the C-terminal side of the same tryptophan residue. These results are rationalized.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200010411
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  • 5
    Electronic Resource
    Electronic Resource
    Morphogens from Dictyostelium discoideum (1988)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 16 (1988), S. 353-355 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The morphogen, DIF-1, from Dictyostelium discoideum has recently been characterized as 1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)-1-hexanone. Two related differentiation-inducing factors, DIF-2 and DIF-3, have been identified as the butyl ketone and monochloro analogues of DIF-1, respectively. These substances together with a number of structural analogues have been synthesized and subsequently analysed by mass spectrometry and bioassay.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200160169
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  • 6
    Electronic Resource
    Electronic Resource
    Fast atom bombardment mass spectral search for the amino terminus of genetically engineered α1-antitrypsin (1988)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 16 (1988), S. 191-195 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Protein structure determination of genetically engineered α1-antitrypsin was carried out using the technique of ‘fast atom bombardment (FAB) MAPPING’. CNBr, tryptic and chymotryptic FAB MAPS were produced. The anticipated amino terminal region of the molecule was not mapped at the expected mass, raising the possibility of post-translational modification. A specific experiment was designed to isolate and identify this region by FAB mass spectral screening of high-performance liquid chromatography separated peptides. A signal at m/z 1231 was observed which could not be assigned to any sequence in the molecule using the computer program. Following CNBr treatment, this signal disappeared completely, giving rise to a new signal at m/z 1058. The amino terminus was thus found to be extended by the presence of an N-acetyl methionine residue, and this discovery is the subject of the present paper; another modification within the sequence will be reported elsewhere. Combining the FAB MAPPING data, the overall structural confirmation achieved was 93% of the recombinant α1-antitrypsin molecule.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200160134
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