منابع مشابه
Comparative serology of two clinical isolates of Bacteroides fragilis and Bacteroides thetaiotaomicron.
Antiserum prepared in rabbits against Bacteroides fragilis showed numerous bands when reacted with B. fragilis antigen in Ouchterlony plates. This antiserum also reacted with Bacteroides thetaiotaomicron and showed one band of apparent identity with B. fragilis. The band of identity common for both organisms was lost if the antigen was heated at 80 degrees C for 30 min. Antisera prepared agains...
متن کاملComparison of the sphingolipid content of rumen Bacteroides species.
Ten strains of Bacteroides ruminicola were found to contain phosphosphingolipids. Four strains of Bacteroides amylophilus and one strain each of Bacteroides succinogenes and Bacteroides sp. were devoid of phosphosphingolipids.
متن کاملGenetic Transformation of Amylase Gene to Ruminal Bacteroides Species Using Conjugation Consequence for Improvement of Rumen Enzyme
Rumen bacterial strains can potentially be manipulated to perform functions different from wild type species. The most numerous species of bacteria in the rumen and gut are species of the familyBacteroidetes, whichcan have the potential for genetic modification for enzyme production. One of the genetic manipulation of rumen bacteria can perform for production of starch digestive enzyme for the ...
متن کاملCulture and physiology of a starch-digesting bacterium (Bacteroides amylophilus n. sp.) from the bovine rumen.
Studies in this and other laboratories have disclosed a variety of starch-digesting rumen organisms, including Streptococcu bouis (Hungate et al., 1952), several cellulolytic strains (Hungate, 1950), and various non-cellulolytic bacteria (Gall et al., 1947; Gall and Huhtanen, 1951; Huhtanen and Gall, 1953a, b; Bryant and Burkey, 1953a,b; Jayko, 1953; McPherson, 1953; van der Wath, 1948) as well...
متن کاملDegradation of soluble and insoluble proteins by Bacteroides amylophilus protease and by rumen microorganisms.
Various soluble and insoluble proteins (6.25 mg) were incubated at 37 C with partially purified protease from Bacteroides amylophilus (156 micrograms) in 2.0 ml of .1 M potassium phosphate buffer, pH 7.6, for 2, 4, 6 and 18 hr, and the liberated amino acids were determined by the ninhydrin method. Results showed that (1) although soluble, serum albumin and ribonuclease A were resistant to hydro...
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ژورنال
عنوان ژورنال: Journal of General Microbiology
سال: 1971
ISSN: 0022-1287
DOI: 10.1099/00221287-67-3-273