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Myxobacterial slime and proteolytic activity

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Abstract

An extracellular protein-polysaccharide-lipide (PPL) complex from exponentially growing cultures of Myxococcus virescens was purified by phosphate precipitation and gel chromatography. The high molecular weight slime polymer appeared homogenous upon isoelectric focusing. The PPL complex exhibited proteolytic activity against gelatin and the activity was only partly reduced by heat treatment. The function of the slime polymer as protein denatured was studied. The complex formed micelles similar to anionic detergents and it inhibited the precipitation and coagulation of proteins by trichloroacetic acid. Lysozyme was totally inactivated when treated with the PPL complex. By gel chromatography binding studies, the PPl complex was found to bind lysozyme in the ratio of 1 to 5.8 (w/w). After separation of added protein from the complex the anticoagulation effect on the protein remained. The biological function of the PPL complex was demonstrated with hemoglobin. When all susceptible peptide bonds in PPL-treated hemoglobin were hydrolyzed by trypsin only 20% in the urea-denatured protein were attacked. The combined role of slime and proteolytic activity is discussed.

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Abbreviations

PPL:

protein-polysaccharide-lipide

TCA:

trichloroacetic acid

BSA:

bovine serum albumin

Tris:

tris-(hydroxymethyl)aminomethane

CMC:

critical micelle concentration

DNFB:

2,4-dinitrofluorobenzene

DNP:

N-dinitrophenyl

SDS:

sodium dodecylsulphate

H.U.:

Hultin units

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  1. Department of Microbiology, University of Lund, Sölvegatan 21, S-223 62, Lund, Sweden

    Gösta Gnosspelius

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  1. Gösta Gnosspelius
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Gnosspelius, G. Myxobacterial slime and proteolytic activity. Arch. Microbiol. 116, 51–59 (1978). https://doi.org/10.1007/BF00408733

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