Fast atom bombardment mass spectrometry and chemical analysis in determinations of acyl‐blocked protein structures

FEBS Letters

Holmquist, Barton²  Jefferey, Jonathan³  Estonius, Mats¹  Parés, Xavier⁴  Vallee, Bert²  Egestad, Börje¹  Persson, Bengt¹  Cederlund, Ella¹  Kaiser, Rudolf¹  Danielsson, Olle¹  Jörnvall, Hans¹ 

[1] Department of Physiological Chemistry, Karolinska Institutet, S-104 01 Stockholm, Sweden;Center for Biochemical and Biophysical Sciences and Medicine, Harvard University, Boston, MA 02115, USA;Department of Molecular and Cell Biology, University of Aberdeen, Marischal College, Aberdeen, AB9 1AS, UK;Departament de Bioquìmica i Biologia Molecular, Universitat Autònoma de Barcelona, Bellaterra, Spain

关键词: Mass spectrometry;    Fast atom bombardment;    Blocked peptide;    N-terminal acetylation;    C-terminal determination;   

DOI  :  10.1016/0014-5793(90)81152-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Peptide generation and fast atom bombardment mass spectrometry in combination with conventional chemical analysis was used to identify the blocking group and establish the N-terminal structure of six different proteins at the nanomole level. In this manner, the first terminal structures of three non-mammalian alcohol dehydrogenases were determined, demonstrating the presence of N-terminal acetylation in these piscine, amphibian, and avian enzymes. Similarly, two different yeast glucose-6-phosphate dehydrogenases and a minor variant of a human alcohol dehydrogenase were found to be acetylated. The exact end location of C-terminal structures was also established. Together, the analyses permit the definition of terminal regions and blocking groups, thus facilitating the delineation of remaining structures.

【 授权许可】

Unknown