Abstract
Quie, Paul G. (University of Minnesota, Minneapolis) and Lewis W. Wannamaker. Staphylococcal Muller phenomenon: relationship to the plasminogen-plasmin system. J. Bacteriol. 82:770–783. 1961.—The staphylococcal factor that produces particulate proteolysis (Muller phenomenon) in whole blood or hemoglobinserum agar plates has been obtained in supernatants from broth cultures. This has facilitated study of the phenomenon in a sterile system. The bacterial factor has been partially separated from other extracellular products by starch zone electrophoresis.
Staphylococcal Muller factor and staphylokinase are similar in heat stability, in electrophoretic mobility, and in activation of a serum proteolytic system. A relationship of the Muller phenomenon to the plasminogen-plasmin system is also suggested by the observation that purified plasminogen may be substituted for serum in the sterile system, and by the finding that inhibitors of the plasminogen-plasmin system also inhibit the Muller phenomenon. Although growing colonies of streptococci fail to exhibit the Muller phenomenon, particulate proteolysis can be demonstrated with streptokinase, using a double-diffusion technique. A similar phenomenon can be produced with urine, suggesting that urokinase may substitute for the bacterial activators in the Muller phenomenon.
Although evidence from other sources suggests that the serum Muller factor is particulate, the serum factor appears to be freely diffusible in agar and is not readily sedimented in the ultracentrifuge.
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- ALKJAERSIG N., FLETCHER A. P., SHERRY S. The mechanism of clot dissolution by plasmin. J Clin Invest. 1959 Jul;38(7):1086–1095. doi: 10.1172/JCI103885. [DOI] [PMC free article] [PubMed] [Google Scholar]
- ELEK S. D. Studies on the proteoclast (Muller's phenomenon). J Hyg (Lond) 1953 Mar;51(1):125–139. doi: 10.1017/s0022172400015540. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fisk R. T., Mordvin O. E. Digestion of Casein by Staphylococci on Milk Agar Containing Serum. J Bacteriol. 1943 Oct;46(4):392–393. doi: 10.1128/jb.46.4.392-393.1943. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HAGAN J. J., ABLONDI F. B., DE RENZO E. C. Purification and biochemical properties of human plasminogen. J Biol Chem. 1960 Apr;235:1005–1010. [PubMed] [Google Scholar]
- KLINE D. L. The purification and crystallization of plasminogen (profibrinolysin). J Biol Chem. 1953 Oct;204(2):949–955. [PubMed] [Google Scholar]
- KUNKEL H. G., SLATER R. J. Zone electrophoresis in a starch supporting medium. Proc Soc Exp Biol Med. 1952 May;80(1):42–44. doi: 10.3181/00379727-80-19516. [DOI] [PubMed] [Google Scholar]
- KUNKEL H. G., TISELIUS A. Electrophoresis of proteins on filter paper. J Gen Physiol. 1951 Sep;35(1):89–118. doi: 10.1085/jgp.35.1.89. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LEWIS J. H., FERGUSON J. H., JACKSON B. G. Bacterial activators (lysokinases) of the fibrinolytic enzyme system of serum. Proc Soc Exp Biol Med. 1949 Dec;72(3):703–706. doi: 10.3181/00379727-72-17549. [DOI] [PubMed] [Google Scholar]
- McCARTY M. The inhibition of streptococcal desoxyribonuclease by rabbit and human antisera. J Exp Med. 1949 Dec;90(6):543–553. doi: 10.1084/jem.90.6.543. [DOI] [PMC free article] [PubMed] [Google Scholar]
- SHERRY S., FLETCHER A. P., ALKJAERSIG N. Fibrinolysis and fibrinolytic activity in man. Physiol Rev. 1959 Apr;39(2):343–382. doi: 10.1152/physrev.1959.39.2.343. [DOI] [PubMed] [Google Scholar]
- WANNAMAKER L. W. Electrophoretic studies of the extracellular products of group A Streptococci. J Exp Med. 1958 Jun 1;107(6):783–795. doi: 10.1084/jem.107.6.783. [DOI] [PMC free article] [PubMed] [Google Scholar]
- WILSON A. T., BRUNO P. The sterilization of bacteriological media and other fluids with ethylene oxide. J Exp Med. 1950 May 1;91(5):449–458. doi: 10.1084/jem.91.5.449. [DOI] [PMC free article] [PubMed] [Google Scholar]