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91.
92.
A serine proteinase possessing a fibrinolytic activity was isolated from a culture filtrate of Streptomyces spheroides, strain 35. A consecutive use of affinity chromatography on bacillichin-silochrome and bacitracin-sepharose and ion-exchange chromatography on anionie PAP and cationic KMT resulted in a homogeneous proteinase with 1060-fold purification and 19% yield. The enzyme has a molecular weight of 28000; its amino acid composition is Asp31, Ser28, Thr29, Glu9, Pro14, Gly35, Ala42, Val26, Ile14, Leu13, Met2, Tyr9, Phe4, Trp3, His6, Lys4, Arg10. The enzyme has a pI at pH greater than 10 and the activity optimum against Z-L-Ala-L-Ala-L-Leu-pNA at pH 10-11. The enzyme is stable within the pH range of 4-11 and in 6 M guanidinium chloride pH 8.0 in the presence of Ca2+. The enzyme is inhibited by diisopropylfluorophosphate and benzylsulfofluoride, specific inhibitors of serine proteinases as well as by potato proteinase inhibitor. The serine proteinase SSPB isolated from Str. spheroides, strain 35 can be related to subtilisin-like serine proteinase, especially to those of SGPD and SGPE of Str. griseus.  相似文献   
93.
The comparative study of the immunological activity of Proteus vaccine prepared from soluble antigenic complexes was made after the immunization of volunteers with this vaccine used in the form of a single preparation and in combination with pyoimmunogen (Pseudomonas aeruginosa vaccine) and/or adsorbed staphylococcal toxoid. The injection of the vaccine in the form of a single preparation and in different combinations increased the ingestion of Proteus cells by neutrophils. The injection of Proteus vaccine simultaneously with pyoimmunogen and staphylococcal toxoid ensured the intensive phagocytosis of staphylococci. All combinations with Proteus vaccine, used in this investigation, stimulated the intensive formation of antibodies to Proteus vaccine strain and Re-glycolipid. Proteus vaccine introduced in combination with adsorbed staphylococcal toxoid essentially stimulated the synthesis of anti-alpha-staphylolysin.  相似文献   
94.
Interactions of the calcium binding proteins, like parvalbumins pI 4.2 and p15.0 and bovine and human alpha-lactalbumins, with dipalmitoylphosphatidylcholine vesicles have been studied by means of scanning microcalorimetry and intrinsic tryptophan, tyrosine and phenylalanine fluorescence. The interactions are modulated by the Ca2+ and Mg2+ binding to the proteins and induce some changes in the physical properties of both the proteins and the liposomes. The liposomes increase the thermal stability of the Mg2+-loaded and metal-free parvalbumin. Ca2+-loaded alpha-lactalbumin interacts with the liposomes in its native state, while the metal-free protein binds to the liposomes mainly in its thermally denatured state. The interactions of both proteins with the liposomes affect the phase transition from gel to liquid-crystalline state in the liposomes. The results of the microcalorimetric and spectrofluorometric studies are corroborated by the data obtained by means of gel-chromatography on Sepharose 4B.  相似文献   
95.
The combined preparation consisting of the antigenic complexes of staphylococci (1 part), Proteus (1 part) and P. aeruginosa parts) was capable of protecting mice from infection with staphylococci, Proteus and P. aeruginosa and prolonging the survival time of rabbits under the conditions of the development of staphylococcal sepsis. The staphylococcal component of the combined preparation possessed adjuvant activity, increasing the immunogenicity of Proteus antigen. The combined vaccine enhanced a short-time increase in the nonspecific resistance of the animals. The moderate toxicity of the preparation permits making multiple injections of the preparation to mice without inhibiting the weight gain of the animals.  相似文献   
96.
Ohne ZusammenfassungAls Dissertation der Universität München angenommen.  相似文献   
97.
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