Circular dichroism of stem bromelain : a third spectral class within the family of cysteine proteinases

Two forms of stem bromelain (EC 3.4.22.4) were isolated from commercial, crude and chromatographically purified preparations of the enzyme by means of gel-filtration and cation-exchange liquid chromatography. These forms possess nearly identical secondary and tertiary structures, as judged from thei...

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Bibliographic Details
Published in:Biochemical journal 1994-05, Vol.300 (1), p.107-110
Main Authors: ARROYO-REYNA, A, HERNANDEZ-ARANA, A, ARREGUIN-ESPINOSA, R
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Bromelains - chemistry
Bromelains - isolation & purification
Chromatography, Gel
Chromatography, Ion Exchange
Circular Dichroism
Electrophoresis, Polyacrylamide Gel
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
Isoelectric Focusing
Molecular Weight
Protein Structure, Secondary
Spectrophotometry, Ultraviolet
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Summary:Two forms of stem bromelain (EC 3.4.22.4) were isolated from commercial, crude and chromatographically purified preparations of the enzyme by means of gel-filtration and cation-exchange liquid chromatography. These forms possess nearly identical secondary and tertiary structures, as judged from their circular dichroism (c.d.) spectra. The spectral characteristics of stem bromelain suggest that this enzyme belongs to the alpha + beta protein class, as other cysteine proteinases do. In agreement with these results, quantitative estimation of secondary structures yielded amounts similar to those for papain and proteinase omega. However, the bromelain c.d. curve is clearly distinguishable from those reported for papain and proteinase omega, on one hand, and that of chymopapain, on the other. Thus, it is apparent that there are at least three types of c.d. spectra associated with the family of cysteine proteinases.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj3000107