Observations on Precipitins against a Peptidase with Chymotrypsin-Like Activity of &lt;i&gt;Micropolyspora faeni, &lt;/i&gt;in Sera of Cattle Exposed to Mouldy Hay

Nicholet, J; Bannerman, Elisabeth; Krawinkler, M.

doi:10.1159/000162538

Cited by 5 publications

(3 citation statements)

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“…However, the precipitins are chiefly against enzymes with chymotrypsin-like activity. We were able to demonstrate a similar 7 reaction in cattle (16). This immunological reaction against metabolic products of M. faeni was later reaffirmed by Fletcher et al (6) and then by Edwards (5).…”

supporting

confidence: 77%

Extracellular enzymes of Micropolyspora faeni found in moldy hay

Nicolet¹,

Bannerman²

1975

Infect Immun

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supporting

confidence: 77%

Extracellular enzymes of Micropolyspora faeni found in moldy hay

Nicolet¹,

Bannerman²

1975

Infect Immun

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“…In a serological survey they found that 30 out of 33 sera reacted with at least one and up to a maximum of four fractions present in their M. faeni extract. Later, Nicolet et al (27), testing sera from cattle affected with farmer's lung, obtained similar results. These enzymes have also been shown to be released extracellularly on hay during molding and may thus be inhaled as free active enzymes with the moldy hay dust (26).…”

mentioning

confidence: 73%

Isolation and characterization of an enzyme with esterase activity from Micropolyspora faeni

Bannerman¹,

Nicolet²

1976

Appl Environ Microbiol

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The isolation and the characterization of one ofthe enzymes ofMicropolyspora faeni that hydrolyzes the substrate N-benzoyl-DL-phenylalanine-beta-naphthyl ester and that seems to be of medical importance are described. This enzyme (enzyme 1) was isolated with an 86-fold purification by using the following seven steps: ammonium sulfate precipitation, gel filtration through Sephadex G-150, heat treatment, chromatography on diethylaminoethyl-cellulose, rechromatography on diethylaminoethyl-Sephadex, gel filtration through Sephadex G-200, and affinity chromatography. Enzyme 1 has a molecular weight of approximately 500,000 and maximum activity at pH 7.8 to 8.0 and at 20°C. The enzyme is stable between pH 7.5 and 10.5 and at temperatures up to 60°C. Its activity is not inhibited by ethylenediaminetetraacetic acid. It is, however, sensitive to diisopropyl phosphofluoride and phenylmethyl sulfonyl fluoride. These properties and the ability to hydrolyze the esters of phenylalanine, tyrosine, and tryptophan without endopeptidasic activity and no marked proteolytic activity suggest that the enzyme is an esterase.

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“…The extensive work carried on in the past I 0 years on proteases of microbial origin has been recently reviewed [ 7,8]. Different authors have also discussed the production by pathogenic fungi of antigenic proteases with chymotrypsin-like activity in connection with the remarkable parasitic adaptability of some species [ 1, 9,16] .…”

Section: Discussionmentioning

confidence: 99%

Immunochemical investigation of four Saprolegnia species with parasitic activity in fish: Serological and kinetic characterization of a chymotrypsin-like activity

Peduzzi

Bizzozero

1977

Microb Ecol

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The antigenic structure of four aquatic Phycomycetes of the genusSaprolegnia with parasitic activity in fish was analyzed with immunoelectrophoresis and double diffusion techniques. It is shown that these serological tests might represent a valuable criterion for the identification of the fourSaprolegnia species:S. parasitica, S. ferax, S. delica, andS. diclina. A specific chromogenic reaction revealed the presence of a protease with chymotrypsin-like activity among the precipitation arcs obtained after immunoelectrophoresis. Analysis of this proteolytic activity by kinetic assay methods confirmed the results of the serological tests. Moreover estimates of the quantity of enzyme present in the cellular extract and in the culture medium were obtained. A possible relationship between the proteolytic activity and the host-parasite interaction was discussed.

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Observations on Precipitins against a Peptidase with Chymotrypsin-Like Activity of <i>Micropolyspora faeni, </i>in Sera of Cattle Exposed to Mouldy Hay

Cited by 5 publications

References 0 publications

Extracellular enzymes of Micropolyspora faeni found in moldy hay

Extracellular enzymes of Micropolyspora faeni found in moldy hay

Isolation and characterization of an enzyme with esterase activity from Micropolyspora faeni

Immunochemical investigation of four Saprolegnia species with parasitic activity in fish: Serological and kinetic characterization of a chymotrypsin-like activity

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