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PMID: 938483 Published · ppublish English Journal Article

The mechanism of folding of globular proteins. Suitability of a penicillinase from Staphylococcus Aureus as a model for refolding studies.

The Biochemical journal ·Vol. 155 ·No. 2 ·1976-05-01 ·Pages 325-30

Robson B, Pain RH

Abstract

1. A homogeneous preparation of penicillinase (penicillin amido-beta-lactamhydrolase, EC 3.5.2.6) was isolated and purified from cultures of Staphylococcus aureus by a simple two-stage procedure. 2. The native protein contains 20-30% helix as determined by optical-rotatory-dispersion and circular-dichroism measurements. Some 54(+/-5)% of the 13 tyrosine residues are exposed to solvent molecules of diameter 0.44 and 0.94 nm. 3. Conditions that allow full recovery of enzymic activity and native conformation from the fully unfolded state in 4M-guanidinium chloride were defined. 4. Refolding of the protein was shown to be inhibited by intermolecular interaction, by small changes in ionization and by low concentrations (0.025 M) of phenol.

MeSH Terms
Guanidines/pharmacology Kinetics Models, Chemical Penicillinase/analysis,isolation & purification Phenols/pharmacology Protein Conformation/drug effects Staphylococcus aureus/enzymology
Chemicals
Guanidines Phenols Penicillinase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Robson B
Pain R H
References (30)
30 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1550325
Published
1976-05-01
Pages
325-30
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1172838
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1550325 PMC Full Text View journal details
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