Trypsin-like enzyme from Streptomyces 771. Purification and properties of native and immobilized enzyme

Applied Biochemistry and Biotechnology
V I PalubinskasI N Krestyanova

Abstract

Electrophoretically homogeneous proteolytic enzyme with molecular weight 31,500 and pI 3.75 was obtained from a culture medium of Streptomyces 771 by chromatography on N-benzyl chitin adsorbent, subsequent chromatography on CM-cellulose, and preparative isofocusing and chromatography on Sephadex G-75. The enzyme hydrolyzes N-benzoyl-DL-arginine-p-nitroanilide N-benzoyl-DL-lysine-p-nitro-anilide N-benzoyl-DL-arginine ethyl ester, and Na-caseinate. It also exhibits pronounced thrombolytic activity. The activity of the enzyme was suppressed by soya bean inhibitor, but remained unaffected by chelating agents and phenylmethylsulfonyl fluoride. The enzyme was immobilized on aldehyde dextran, and some kinetic parameters of the immobilized enzyme were determined. The thrombolytic activity of native and immobilized enzyme was studied as well.

References

Jan 12, 2008·Analytical Sciences : the International Journal of the Japan Society for Analytical Chemistry·Fumihiko KitagawaKoji Otsuka
Sep 4, 2009·Journal of Biomedical Optics·Mark A MackanosChristopher H Contag
Feb 14, 2014·Analytical Sciences : the International Journal of the Japan Society for Analytical Chemistry·Hirosuke HatayamaMasanori Fujinami

Citations

Jan 1, 1972·Methods in Enzymology·K WeberM Osborn
Sep 24, 1969·Biochemical and Biophysical Research Communications·L JurasekL B Smillie
Sep 10, 1968·Archives of Biochemistry and Biophysics·K Morihara, H Tsuzuki
Jun 10, 1971·FEBS Letters·N YoshidaH Inoue
Dec 28, 1964·Annals of the New York Academy of Sciences·B J DAVIS

Related Concepts

Bacterial Proteins
Trypsin Inhibitors
SDS-PAGE
Peptide Hydrolases
Endopeptidases
Metalloendopeptidases
Trypure
Streptomyces

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