On the Purity of 3X-Recrystallised Bovine α-Chymotrypsin
The results of an electrospray-mass spectrometric analytical study of aqueous solutions of fifteen commercial samples of 3X-recrystallised bovine α-chymotrypsin are presented and discussed. It was found that only six samples were predominantly α-chymotrypsin and that two samples contained no α-chymo...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1993-04, Vol.192 (1), p.75-81 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Ashton, D.S. Beddell, C.R. Cooper, D.J. Green, B.N. Oliver, R.W.A. Welham, K.J. |
| description | The results of an electrospray-mass spectrometric analytical study of aqueous solutions of fifteen commercial samples of 3X-recrystallised bovine α-chymotrypsin are presented and discussed. It was found that only six samples were predominantly α-chymotrypsin and that two samples contained no α-chymotrypsin at all. The remaining seven samples were found to be mixtures of α-chymotrypsin with other chymotrypsins and, in some cases, neochymotrypsinogens. The majority of the results are rationalised in terms of previously postulated and/or observed products of proteolytic activation of bovine chymotrypsinogen A. However, evidence is also presented for the presence in many of the samples of three new serine proteases, of significantly lower molecular masses than α-chymotrypsin, which cannot at present be explained. The paper is concluded with a brief discussion of the implications of the analytical findings for enzymological studies. |
| doi_str_mv | 10.1006/bbrc.1993.1383 |
| format | Article |
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It was found that only six samples were predominantly α-chymotrypsin and that two samples contained no α-chymotrypsin at all. The remaining seven samples were found to be mixtures of α-chymotrypsin with other chymotrypsins and, in some cases, neochymotrypsinogens. The majority of the results are rationalised in terms of previously postulated and/or observed products of proteolytic activation of bovine chymotrypsinogen A. However, evidence is also presented for the presence in many of the samples of three new serine proteases, of significantly lower molecular masses than α-chymotrypsin, which cannot at present be explained. 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| ispartof | Biochemical and biophysical research communications, 1993-04, Vol.192 (1), p.75-81 |
| issn | 0006-291X 1090-2104 |
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| source | ScienceDirect Journals (5 years ago - present) |
| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases |
| title | On the Purity of 3X-Recrystallised Bovine α-Chymotrypsin |
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