Evidence for two molecular forms of streptococcal erythrogenic toxin. Conversion to a single form by 2-mercaptoethanol.

Two molecular forms of streptococcal erythrogenic toxin have been isolated by DEAE-cellulose chromatography. These two forms exhibit the same biological and immunological properties. They have the same sedimentation coefficient s20= 2.52. Molecular weight is about 30 000. The protein is made of a single polypeptide chain with glutamic acid as N-terminal amino acid. Exposure to 2-mercaptoethanol induces conversion to a single form. The possibility that the different molecular forms arise from the binding of small molecules of different charge through a sulfhydryl group of the protein is discussed.

[1]  H. Fraenkel-conrat,et al.  Recent developments in techniques for terminal and sequence studies in peptides and proteins. , 2006, Methods of biochemical analysis.

[2]  C. Markert.  THE MOLECULAR BASIS FOR ISOZYMES , 1968, Annals of the New York Academy of Sciences.

[3]  H. Kirkman,et al.  ISOZYMES OF HUMAN RED CELL GLUCOSE‐6‐PHOSPHATE DEHYDROGENASE * , 1968, Annals of the New York Academy of Sciences.

[4]  N. Kaplan,et al.  NATURE OF MULTIPLE MOLECULAR FORMS OF ENZYMES * , 1968, Annals of the New York Academy of Sciences.

[5]  A. Schechter,et al.  AN APPROACH TO THE PROBLEM OF CONFORMATIONAL ISOZYMES , 1968, Annals of the New York Academy of Sciences.

[6]  A. W. Bernheimer,et al.  Isoelectric analysis of cytolytic bacterial proteins , 1968, Journal of bacteriology.

[7]  C. Markert,et al.  Malate dehydrogenase isozymes of the marine snail, Ilyanassa obsoleta , 1967 .

[8]  H. A. Barker,et al.  Purification and characterization of component S of glutamate mutase. , 1967, The Journal of biological chemistry.

[9]  L. L. Schwartz,et al.  Isolation and composition of staphylococcal alpha toxin. , 1963, Journal of general microbiology.

[10]  D. A. Yphantis.  RAPID DETERMINATION OF MOLECULAR WEIGHTS OF PEPTIDES AND PROTEINS * , 1960 .

[11]  G. Ellman,et al.  Tissue sulfhydryl groups. , 1959, Archives of biochemistry and biophysics.

[12]  F. S. Scanes,et al.  Products of hydrolysis of dinitrophenylproline and N-terminal proline-peptides with hydrochloric acid. , 1956, The Biochemical journal.

[13]  C. Hanes,et al.  Enzymic transpeptidation reactions involving γ-glutamyl peptides and α-amino-acyl peptides , 1952 .

[14]  J. F. Foster,et al.  The microheterogeneity of plasma albumins. V. Permutations in disulfide pairings as a probable source of microheterogeneity in bovine albumin. , 1969, Biochemistry.

[15]  J. Monod,et al.  On the determination of molecular weight of proteins and protein subunits in the presence of 6 M guanidine hydrochloride. , 1968, Biochemistry.

[16]  K. Erismann.  Hilfsmittel zum Arbeiten mit radioaktiven Substanzen in der Dünnschicht-chromatographie , 1965 .

[17]  R. Munier,et al.  Procédé de chromato-électrophorése permettant d'obtenir la séparation des dinitrophényl-aminoacids hydrosolubles , 1963 .

[18]  G. Biserte,et al.  Chromatographie sur papier des dinitrophénylaminoacides , 1959 .

[19]  D. Phillips.  The N-terminal groups of calf-thymus histones. , 1958, The Biochemical journal.

[20]  Bettelheim Fr.  Amino terminal group in chymotrypsinogen. , 1955 .