Novel Leu-Lys-specific peptidase (leulysin) produced by gel-entrapped yeast cells

Tsutomu Okada; Kenji Sonomoto; Atsuo Tanaka

doi:10.1016/0006-291X(87)91323-4

Novel Leu-Lys-specific peptidase (leulysin) produced by gel-entrapped yeast cells

Tsutomu Okada, Kenji Sonomoto, Atsuo Tanaka

Research output: Contribution to journal › Article › peer-review

7 Citations (Scopus)

Abstract

Saccharomyces cerevisiae cells entrapped with a neutral hydrophilic photo-crosslinkable resin prepolymers specifically excreted into a cultured medium a new type of a peptidase, which cleaved Leu-Lys bond of α-mating factor. The enzyme was purified by membrane filtration followed by ion exchange chromatography and gel filtration chromatography. The purified enzyme showed a strict substrate specificity on internal Leu-Lys bond. Leu-Lys bond near terminus of a molecule and Leu-X and X-Lys bonds examined so far were not hydrolyzed by the enzyme.

Original language	English
Pages (from-to)	316-322
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	145
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(87)91323-4
Publication status	Published - May 29 1987
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(87)91323-4

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abstract = "Saccharomyces cerevisiae cells entrapped with a neutral hydrophilic photo-crosslinkable resin prepolymers specifically excreted into a cultured medium a new type of a peptidase, which cleaved Leu-Lys bond of α-mating factor. The enzyme was purified by membrane filtration followed by ion exchange chromatography and gel filtration chromatography. The purified enzyme showed a strict substrate specificity on internal Leu-Lys bond. Leu-Lys bond near terminus of a molecule and Leu-X and X-Lys bonds examined so far were not hydrolyzed by the enzyme.",

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AU - Okada, Tsutomu

AU - Sonomoto, Kenji

AU - Tanaka, Atsuo

PY - 1987/5/29

Y1 - 1987/5/29

N2 - Saccharomyces cerevisiae cells entrapped with a neutral hydrophilic photo-crosslinkable resin prepolymers specifically excreted into a cultured medium a new type of a peptidase, which cleaved Leu-Lys bond of α-mating factor. The enzyme was purified by membrane filtration followed by ion exchange chromatography and gel filtration chromatography. The purified enzyme showed a strict substrate specificity on internal Leu-Lys bond. Leu-Lys bond near terminus of a molecule and Leu-X and X-Lys bonds examined so far were not hydrolyzed by the enzyme.

AB - Saccharomyces cerevisiae cells entrapped with a neutral hydrophilic photo-crosslinkable resin prepolymers specifically excreted into a cultured medium a new type of a peptidase, which cleaved Leu-Lys bond of α-mating factor. The enzyme was purified by membrane filtration followed by ion exchange chromatography and gel filtration chromatography. The purified enzyme showed a strict substrate specificity on internal Leu-Lys bond. Leu-Lys bond near terminus of a molecule and Leu-X and X-Lys bonds examined so far were not hydrolyzed by the enzyme.

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Novel Leu-Lys-specific peptidase (leulysin) produced by gel-entrapped yeast cells

Abstract

All Science Journal Classification (ASJC) codes

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