On the analysis of bovine trypsin by electrospray-mass spectrometry

• Published in: Biochemical and biophysical research communications Vol. 199; no. 2; p. 694
• Main Authors: Ashton, D S, Ashcroft, A E, Beddell, C R, Cooper, D J, Green, B N, Oliver, R W
• Format: Journal Article
• Language: English
• Published: United States 15-03-1994
• Subjects: Animals; Cattle; Chickens; Horses; Mass Spectrometry - methods; Molecular Weight; Muramidase - chemistry; Myoglobin - chemistry; Trypsin - chemistry
• ISSN: 0006-291X
• DOI: 10.1006/bbrc.1994.1284

In this paper the results obtained from an electrospray mass spectrometric (ES-MS) analytical study of commercial grade bovine trypsin are presented and discussed. It is proven, somewhat contrary to an earlier report, that ES-MS analysis may be performed routinely on a triple quadrupole mass spectrometer using the normal ES-MS raw data transformation procedures to identify and quantify the three forms of trypsin, namely, beta, alpha and psi, present in the samples. Further, it was found that all of the samples analysed contained small amounts of two peptides of M(r) = 5447 and 17,882 Da, which are postulated to originate from catalytic cleavage of alpha-trypsin by beta-trypsin.