The characterization of two new low molecular weight proteins (LMPs) from Streptococcus pyogenes.

Two novel extracellular mitogenic substances were isolated from Streptococcus pyogenes strain NY-5 and characterized. The purification steps involved an initial enrichment of the proteins from culture supernatant by silica gel adsorption, followed by ion exchange chromatography and gel filtration. The purified materials were homogeneous in SDS-PAGE, showed estimated molecular weights of 12 kD and isoelectric points of 4.

Amino acid analysis of selected reversed-phase high performance liquid chromatographic peaks of crude and partially purified lysed human leukocyte ultrafiltrate.

Analytic reversed-phase high performance liquid chromatography (RP-HPLC) was performed to separate from the crude lysed human leukocyte ultrafiltrate (LLU) its partially purified most immunoactive subfraction P2/II in vivo. Under conditions used, the highest degree of segregation of both. LLU and P2/II could be observed in the first, as well as in the last two fifth of the water-methanol gradient.

Type 1 and 3 M-proteins of Streptococcus pyogenes: peptic extraction and fibrinogen binding properties.

The pepsin extraction of group A type 1 streptococci for the isolation of M protein fragments was studied at different pH values and at different time intervals. The extracts were compared by SDS PAGE and fused rocket immunoelectrophoresis. Type 1 M protein fragments were prepared in preparative scale by pepsin extraction of type 1 streptococci at pH 5.

Purification and characterization of Streptococcus pyogenes erythrogenic toxin type A produced by a cloned gene in Streptococcus sanguis.

The gene of Streptococcus pyogenes erythrogenic toxin type A (speA) has been previously cloned in Streptococcus sanguis (Challis) and produces extracellular erythrogenic toxin type A (ET A). The ET A produced and secreted by this heterologous host was purified to homogeneity and shown to have properties identical to ET A produced by S. pyogenes strain NY-5; i.

Type 1 M protein of Streptococcus pyogenes. N-terminal sequence and peptic fragments.

Limited proteolysis of the surface of type 1 Streptococcus pyogenes by pepsin gives rise to fragment Pep M1 of Mr 20270 as the main product which covers the N-terminal part of the M protein. The amino acid sequence was determined of the N-terminal region of the M protein representing the most exposed part of the molecule on the surface fibrils of streptococcal cells, which seems to be very important for the differentiation of the individual serological types. The sequence differs from the homologous N-terminal sequences of types 5, 6 and 24, and shows a homology with sequences repeating in the chain of type 24.