New Pepsin Inhibitors (S-PI) from<i>Streptomyces</i>EF-44-201

Murao, Sawao; Satoi, Shūzō

doi:10.1080/00021369.1970.10859764

Cited by 19 publications

(13 citation statements)

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“…One unit of enzyme activity was defined as the generation of 1 µmol tyrosine per min (Eguchi & Iwamoto, 1976). The following proteinase inhibitors were used in experiments on the inhibition of proteinase activity : iodoacetic acid, PMSF, o-phenanthroline, E-64 [trans-epoxysuccinylamido(4-guanidino)-butane], S-PI (Murao & Satoi, 1970), antipain, chymostatin, leupeptin and talopeptin (Murao et al, 1980). Purification of proteinase in the haemolymph.…”

Section: Methodsmentioning

confidence: 99%

Efficient protein production using a Bombyx mori nuclear polyhedrosis virus lacking the cysteine proteinase gene.

Suzuki¹,

Kanaya

Okazaki

et al. 1997

Journal of General Virology

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Infection by a baculovirus (Bombyx mori nuclear polyhedrosis virus, BmNPV) in silkworm (Bombyx mori) larvae is highly efficient as an expression system for the production of useful proteins. However, the amount of the protein of interest expressed tends to decrease in the later stages of infection presumably due, in part, to a proteinase produced in the larval haemolymph. The N-terminal amino acid sequence of a proteinase purified from the haemolymph of BmNPV-infected larvae was identical to the internal amino acid sequence of the viral cysteine proteinase gene of BmNPV, suggesting that the cysteine proteinase in the haemolymph originated from the BmNPV gene. We constructed a

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Section: Methodsmentioning

confidence: 99%

Efficient protein production using a Bombyx mori nuclear polyhedrosis virus lacking the cysteine proteinase gene.

Suzuki¹,

Kanaya

Okazaki

et al. 1997

Journal of General Virology

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“…CM-Sepharose CL-6B, Sephadex G-IOO, protein standards for molecular weight calibration, and Pharmalyte were purchased from Pharmacia Fine Chemicals Co., Sweden. SSI, 11) MAPI, 12) Talopeptin, I 3) and S-PI 14) were purified by the methods ofMurao et al Cbz-Ala-Ala-Xaa (Xaa = Leu or Phe)-NphN0 2 were synthesized in this laboratory. API-2 IS ) was a kind gift of Prof. Dr. M. Uyeda, Kumamoto University, Kumamoto, Japan.…”

Section: Methodsmentioning

confidence: 99%

Isolation and Characterization of a Serine Proteinase, Inactivating m-Subunit of Lactate Dehydrogenase, fromPenicillium citrinumKE-1

Watazu¹,

Nagamatsu²,

Shirahase³

et al. 1994

Bioscience, Biotechnology, and Biochemistry

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A selective inactivating enzyme for the m-subunit of lactate dehydrogenase (LDH) was found in the culture filtrate of Penicillium citrinum KE-1, newly isolated from soil. The enzyme was purified from the culture filtrate by ammonium sulfate fractionation, column chromatography on CM-Sepharose CL-6B, and gel filtration on Sephadex G-100. The purification was 124-fold with an activity yield of 81%. The purified enzyme gave a single band, corresponding to a molecular weight of 32,000, on SDS polyacrylamide gel electrophoresis, and the isoelectric point was 9.5. The enzyme specifically inactivated the m-subunit of LDH but showed no activity on the h-subunit of LDH. The enzyme, named KE-1 proteinase, proved to be a serine-type proteinase. Limited proteolysis of native m-subunit of LDH was assumed to result in a loss of enzyme activity.

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“…These enzymes were markedly inactivated by NBS and 1 2 , d) Effect of Streptomyces-pepsin inhibitor (S_PI). 16,17) Effects of S-PI on these acid proteases were tested, comparing with various acid proteases at optimum pH.…”

Section: ) Homogeneity Of the Enzyme Preparation A) Ultracentrifugalmentioning

confidence: 99%

Purification and Some Enzymatic Properties of Acid Protease A and B ofScytalidium lignicolumATCC 24568

Oda

Murao

1974

Agricultural and Biological Chemistry

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New Pepsin Inhibitors (S-PI) fromStreptomycesEF-44-201

Cited by 19 publications

References 0 publications

Efficient protein production using a Bombyx mori nuclear polyhedrosis virus lacking the cysteine proteinase gene.

Efficient protein production using a Bombyx mori nuclear polyhedrosis virus lacking the cysteine proteinase gene.

Isolation and Characterization of a Serine Proteinase, Inactivating m-Subunit of Lactate Dehydrogenase, fromPenicillium citrinumKE-1

Purification and Some Enzymatic Properties of Acid Protease A and B ofScytalidium lignicolumATCC 24568

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