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At least 1,135 records · Page 63Linked to original sources
PubMed1975

[Study of the population makeup and antibiotic and transamidinase activity of Actinomyces streptomycini 773 stored for a long period in a lyophilized, dried state].

Studies on variation of the streptomycin-producing organism Act. streptomycini 773 on its storage in lyophilized state showed that prolonged maintenance (for 8 years) resulted in increased percentage of "oligospore" (up to 6.9 per cent) and asporogenic (up to 6.0 per cent) variants in the population. The variants had lower transamidinase and antibiotic activity.

Actinomyces↗
PubMed1975

[Variability of the levorin producer, Actinomyces levoris Krass].

Natural variation of the levorin-producing organism Act. levoris, strain 28 was studied with respect to the colony morphology and production of levorin and levoristatin. The population of strain 28 consisted of 3 morphological colony types, the main type amounting to 99.7 percent. The strain variation with respect to production of levorin and levoristatin ranged from 20 to 180 and from 0 to 300 percent respectively as compared to the control. Mutant M-28 differing from the initial strain by the colony morphology, moderate phage titer and preferable production of levoristatin was isolated as a result of repeated passages of strain 28 onto agarized Chapek media with starch without maintaining selection. Variants differing from the population of strains 28 and M-28 by the ratio of levorin and levoristatin in the culture fluid were selected. No correlation in production of the above antibiotics by strain 28 was noted. Preparations obtained with strain M-28 differed from those obtained with strain 28 in a significant content of levoristatin.

Actinomyces↗
PubMed1997

[The study of actinomyces viscosus adhere to teeth. III. The identification of mutants of A. viscosus and preparation of rabbit IgG against type 1 and type 2 fimbriae].

The authors prepared rabbit antisera against 5519 and 5951. The IgGs against type 1, type 2 fimbriae were purified from the antisera using sera absorbed with the other strain and IgG purification method. It was identified by SDS-PAGE and ELISA. This result suggested the purified proteins were the IgG against type 1 and type 2 fimbriae.

Actinomyces viscosus↗
PubMed1997

[The study of actinomyces viscosus adhere to teeth. IV. The study of salivary protein receptors of A. viscosus].

In order to determine the receptors of A. viscosus for adhesion, 7 kinds of main purified proteins from pellicle formed by whole saliva were tested. The result indicated that: 1. APRP, statherin, PRPG and SIgA were the receptors of standard and fresh isolated A. viscosus; 2. APRP and stather promoted the adherence of 5519 (1+2-) to HA, and SIgA promoted the adherence 5951 (1-2+) to HA; PRPG was the common receptor of the two fimbriae. It suggested that there were receptors not only type 1 fimbriae but also type 2 in pellicle. Two types of fimbriae were involved in the adherence of A. viscosus to pellicle. The difference existed in the receptor of adherence and the activity site of the same receptor.

Actinomyces viscosus↗
PubMedDate not supplied

[Composition of lipids of Actinomyces olivaceus--synthesis of vitamin B 12].

Total cellular lipids of the synthetic of vitamin B12 Act. olivaceus involve predominantly phospholipids (about 70%). Lipid phosphates consist of phosphatidyl ethanol amine and phosphatidyl-2,3-butandiol (over 40 and 30%, respectively) and lower quantities of phosphatidyl inositol olmonomanoside and cardiolipin. The neutral fraction includes the predominating fraction of triglycerides (over 20%) as well as mono- and diglycerides, free fatty acids, hydrocarbons and three fractions similar to waxes, sterines and sterine esters in their Rf values.

Actinomyces↗
PubMed1979

[Elastolytic enzymes from Actinomyces fradiae 119].

Using ion-exchange chromatography and gel-filtration, elastase II, the main elastolytic component of protofradin (preparation of proteases of Act. fradiae 119), was purified to an electrophoretically homogeneous state. The enzyme is a serine proteinase with mol. weight of 17800 +/- 1000 and a pI greater than 10. The enzyme is stable at pH greater than 4,0 and exhibits its maximal activity towards elastin at pH 9,2. An analysis of elastolytic products revealed that the enzyme hydrolyses natural elactin of bovine nuchal ligament to form large fragments with mol. weights ranging from 25 000 to 80 000 and small oligopeptides. The elastolysis is ceased at the stage of formation of short-chained peptides, predominantly tripeptides. Elastase I is a minor component of protofradin and in its molecular weight and some enzymatic properties is similar to elastase II.

Actinomyces↗
PubMed1999

[A study on the biological properties of fimbriae of Actinomyces viscosus. I. The preparation and determination of fimbriae of A. viscosus].

OBJECTIVE: To build up the methods to prepare and determine the fimbriae of A. viscosus. METHODS: Type 1 and 2 fimbriae were prepared from A. viscosus 5519 and 5951 respectively. Fimbriae were isolated from bacteria cells by mechanical shaking, obtained by collecting the supernatant after centrifugation, and purified by ammonium sulfate precipitations and gel filtration. RESULTS: Electron microscope showed that fimbriae existed in the preparations. The immunological reaction between the fimbriae preparations and specific antibodies against fimbriae attested that they were type 1 or type 2 fimbriae. CONCLUSION: The present study become a foundation for further study on the biological properties of fimbriae of A. viscosus.

Actinomyces viscosus↗