6533b7d7fe1ef96bd1268290

RESEARCH PRODUCT

Self-assembly properties of the proteinaceous coat secreted by the ?slime? variant of Neurospora crassa

Manuel CasanovaJ. Ruiz-herreraM L GilRafael SentandreuJosé P. Martínez

subject

chemistry.chemical_classificationGel electrophoresisbiologyGeneral Medicinebiology.organism_classificationBiochemistryMicrobiologyIn vitroNeurospora crassaGel permeation chromatographychemistry.chemical_compoundchemistryBiochemistryGeneticsExtracellularGuanidineGlycoproteinMolecular BiologyMacromolecule

description

The proteinaceous extracellular material (PEM) synthesized by the cells of the ‘slime” strain of Neurospora crassa (see Martinez et al. 1989) was solubilized by treatment with urea or guanidine. Removal of these chemicals by dialysis, caused reassembly of the solubilized proteins into material with the same microscopic appearance as the original PEM. Polypeptide patterns from both native and reassembled structures were identical. Dialysis-mediated reassembly of the solubilized proteins appeared to be dependent on both concentration of the soluble macromolecules and time. Gel chromatography of PEM solubilized with different agents revealed two discrete populations of complexes with molecular masses of 1,500 and 500 kDa respectively. These were able to reassemble into lamellar structures with a variable degree of efficiency.

https://doi.org/10.1007/bf00447008