| 7204 |
Triosephosphate isomerase from young and old Turbatrix aceti |
10.1016/0003-9861(76)90352-0. |
Arch Biochem Biophys |
Triosephosphate isomerase from young and old Turbatrix aceti
Abstract
|
| 9554 |
Measures for the rehabilitation of chronic mentally diseased patients |
None |
Lebensversicher Med |
Measures for the rehabilitation of chronic mentally diseased patients
Abstract
|
| 23734 |
Metabolic products of microorganisms. 166. Optimization of the desferri-ferricrocin production by Aspergillus viridi-nutans Ducker & Thrower (author's transl) |
10.1007/BF00446459. |
Arch Microbiol |
Metabolic products of microorganisms. 166. Optimization of the desferri-ferricrocin production by Aspergillus viridi-nutans Ducker & Thrower (author's transl)
Abstract
- At low iron(III)-concentrations (less than 10(-5) M) the fungus Aspergillus viridi-nutans Ducker & Thrower excretes desferri-ferricrocin as the main sideramine into the culture medium. While this compound accounts for 95% of the sideramines produced, small amounts of additional sideramines may also be detected. In a search for an inexpensive nutrient medium for optimum production of desferri-ferricrocin, experiments using shake flasks with good aeration were undertaken initially. The best medium conditions were then employed in a fermentor system. In a 20-1 fermentor with "intensor" system, it was shown that at certain growth rates there was an inverse correlation between rate of growth and rate of sideramine production. A defined nutrient medium of glucose plus acetate as carbon sources, and urea or ammonium acetate as nitrogen sources was used. Two different feeding regimens were used in response to changes of pH or to changes of partial pressure of oxygen in the submerged culture: acetic acid/urea or acetic acid/ammonium acetate additions regulated these conditions. The rate of sideramine production under such feeding achieved a maximum of 20 mg 1(-1) h-1 over a period of several days.
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| 39060 |
Determination of virginiamycin in feeds |
None |
J Assoc Off Anal Chem |
Determination of virginiamycin in feeds
Abstract
- Virginiamycin was extracted from the feed by ethanol-pH 2.5 phosphate buffer (1 + 1). The pH during extraction was adjusted (when necessary) to between 4 and 5. Sample dilutions and the standard dose response line were prepared to contain ethanol pH 6 phosphate buffer (2 + 8), and the test organism was Sarcina lutea. Three feeds (a poultry ration, a swine finishing ration, and a swine starter ration) showed virginiamycin recovery of 88.8--108.9% when standard solutions were added at concentrations of 4.54--90.8 g/ton. The coefficient of variation (4--20%) was larger for low potency feeds (10 g/ton) compared to the higher feeds (100 g/ton). Similarly, excellent recovery was obtained when the swine starter feed was fortified by a commercial premix. Amprolium, roxarsone, and monensin can be present at 20 times the concentration of virginiamycin with little or no interference in the antibiotic determination. Lasalocid at 10 times the concentration of virginiamycin caused a slightly positive bias (recovery, 107.4%).
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| 47290 |
The interaction of actinomycin C3 and actinomine with DNA. A small-angle x-ray scattering study |
10.1111/j.1432-1033.1975.tb03900.x. |
Eur J Biochem |
The interaction of actinomycin C3 and actinomine with DNA. A small-angle x-ray scattering study
Abstract
- Small-angle X-ray scattering was applied to solutions of calf thymus DNA and calf thymus DNA complexed with various amounts of actinomycin C3 or actinomine in phosphate-saline buffer at pH 6.9 and I equals 0.2. From the measurements of DNA in the absence of dye, two cross-section radii of gyration of R-c equals 0.875 plus or minus 0.015 nm and R-c2 equals 0.81 plus or minus 0.02 nm, and a mass per unit length of M/l equals 1906 plus or minus 43 daltons/nm resulted. The investigation of DNA complexed with dye revealed a decrease of the cross-section radii of gyration as compared to those for the DNA in the absence of dye and a relatively low increase of the mass per unit length on binding of actinomycin and a slight decrease of M/l on binding of actinomine. The latter results are interpreted on the basis of a length increase of the DNA double helix by 0.47 plus or minus 0.03 nm per actinomycin molecule and by 0.355 plus or minus 0.03 nm per actinomine molecule bound. The results for R-c and R-c2 obtained for the various samples of complexed DNA were extrapolated to the limiting binding ratio where each dye molecule is associated with a minimum of six nucleotide pairs. According to this extrapolation, the cross-section radii of gyration of such a complex would amount to (R-c)b equals 0.805 plus or minus 0.015 nm and (R-c2)b equals 0.76 plus or minus 0.015 nm for the complex with actinomycin, and to (R-c)b equals 0.77 plus or minus 0.015 nm and (R-c2)b equals 0.75 plus or minus 0.01 nm for the actinomine complex. On the basis of a core and shell model for solvated DNA, these results can be understood as to indicate a decrease of the radial dimensions of both the core and the shell when the dye is bound. The experimental results are compared with theoretical data calculated from the atomic coordinates of the detailed intercalation model for the actinomycin - DNA complex as recently proposed by Sobell and Jain. The model proves to be consistent fairly well with our data on the length increase of the double helix, but it appears to be unable to explain the experimentally observed decrease of R-c2 on binding of dye.
|
| 49449 |
Critical concentrations for resistances of tubercle bacilli to tuberactinomycin-N, viomycin, capreomycin, and lividomycin in patients treated with these agents (cross-resistance-relationships among resistances to aminoglucoside-antibiotics found during chemotherapy for tuberculosis) (author's transl) |
None |
Kekkaku |
Critical concentrations for resistances of tubercle bacilli to tuberactinomycin-N, viomycin, capreomycin, and lividomycin in patients treated with these agents (cross-resistance-relationships among resistances to aminoglucoside-antibiotics found during chemotherapy for tuberculosis) (author's transl)
Abstract
|
| 50402 |
Cross-resistant relationships among the aminoglucoside antibiotics in Mycobacterium tuberculosis |
10.1099/00221287-88-2-269. |
J Gen Microbiol |
Cross-resistant relationships among the aminoglucoside antibiotics in Mycobacterium tuberculosis
Abstract
- Phenotypes of isolates of Mycobacterium tuberculosis H37RV showing resistance to the aminoglucoside antibiotics streptomycin, viomycin, kanamycin, capreomycin, tuberactinomycin N, lividomycin and paromomycin could be grouped into the following types: (I) resistant only to different levels of streptomycins; (2) resistant only to a low level of kanamycin; (3) triply resistant, to low levels of viomycin, tuberactinomycin N and capreomycin; (4) triply resistant, to a low level of kanamycin and high levels of lividomycin and paromomycin; (5) quadruply resistant, to a low level of capreomycin and high levels of kanamycin, lividomycin and paromomycin; (6) hextuply resistant, to high levels of viomycin, tuberactinomycin N, capreomycin, kanamycin, lividomycin, and paromomycin. Three modificatied types of the latter were also observed. Appearance rates of the six types were estimated as 10(-6) to 10(-9), 10(-6), 10(-6) to 10(-7), 10(-8), 10(-8), and 10(-8) to 10(-9), respectively, in a total viable population of the parent strain. Mutations to all phenotypes were considered to be produced by single mutations. According to cross-resistance relationships, aminoglucoside antibiotics were classified into three groups: (I) streptomycin; (II) viomycin, tuberactinomycin N and capreomycin; (III) kanamycin, lividomycin and paromomycin. No cross-resistance relationship between streptomycin and other antibiotics was observed. Resistances to viomycin, tuberactinomycin N and capreomycin occurred by single mutation to type 3. Resistances to kanamycin, lividomycin and paromomycin occurred by single mutations to types 4 and 5. Low resistance to capreomycin was produced by mutation to type 5. Therefore capreomycin was considered to be an intermediate between the second and third groups. These two groups had a close relationship, as resistance to all six agents in these groups could be produced by a single mutation to type 6 (and its modified types).
|
| 58480 |
Arrhythmias in inflammatory heart disease (author's transl) |
None |
Wien Klin Wochenschr |
Arrhythmias in inflammatory heart disease (author's transl)
Abstract
- A review and discussion of the incidence and clinical importance of various cardiac arrhythmias in patients with inflammatory diseases of the heart is presented in this paper.
|
| 61134 |
The chemical structure of capreomycin |
10.1007/BF01927571. |
Experientia |
The chemical structure of capreomycin
Abstract
- The chemical structure of capreomycin, antituberculous peptide antibiotic, was revised from the results of NMR-analysis in comparison with tuberactinomycins. Capreomycin IA and IB were concluded to possess the similar amino acid sequences in their cyclic peptide moieties to those of tuberactinomycins.
|
| 70202 |
The peptide antibiotics of Bacillus: chemistry, biogenesis, and possible functions |
10.1128/br.41.2.449-474.1977. |
Bacteriol Rev |
The peptide antibiotics of Bacillus: chemistry, biogenesis, and possible functions
Abstract
|
| 118901 |
Exoprotease production by sporogenous and asporogenous mycobacillin non-producer mutants of Bacillus subtilis |
10.1007/BF02927117. |
Folia Microbiol (Praha) |
Exoprotease production by sporogenous and asporogenous mycobacillin non-producer mutants of Bacillus subtilis
Abstract
- Mycobacillin non-producers, whether sporogenous or asporogenous, possess less exoprotease, but effective exoprotease producers are not always good mycobacillin yielders. There might exist a minimum level of exoprotease formation for elaboration of mycobacillin.
|
| 163768 |
Cell-free synthesis of vesicular stomatitis virus proteins: translation of membrane-bound polyribosomal mRNAs |
10.1016/0014-5793(75)80530-8. |
FEBS Lett |
Cell-free synthesis of vesicular stomatitis virus proteins: translation of membrane-bound polyribosomal mRNAs
Abstract
|
| 171273 |
Improved high-performance liquid chromatographic method for polypeptide antibiotics and its application to study the effects of treatments to reduce microbial levels in bacitracin powder |
10.1016/s0021-9673(00)99995-3. |
J Chromatogr |
Improved high-performance liquid chromatographic method for polypeptide antibiotics and its application to study the effects of treatments to reduce microbial levels in bacitracin powder
Abstract
- Improvements were made in the high-performance liquid chromatographic (HPLC) method to obtain baseline separation of chromatographic peaks of structurally similar polypeptide components in bacitracin. The improved method uses a 30-cm-long stainless-stell column packed with muBondapak C18. The theoretical plates of the column are approximately 140,000 per meter for the bacitracin A peak. The resolution function between bacitracins B1 and B2 and that between bacitracins A and B2 have been improved 418 and 225%, respectively. The components of bacitracin, bacitracins A, B, C, D, E, F, and G, were fractionated by the countercurrent distribution technique. These components, together with Compound X, a compound separated on a carboxymethylcellulose column, and bacitracin F, obtained by degrading bacitracin A sample at neutral pH, were used to identify peaks in the HPLC chromatogram. Effects of processing methods used to reduce microbial contamination levels in bacitracin powders were evaluated. Heat treatment caused a significant loss of antimicrobial activity (35% reduction), bacitracins A, B1, and B2 were reduced by 37, 22, and 21%, respectively. A significant increase (2.8 times) of bacitracin F, an oxidative degradation compound, was show. Irradiation by 60Co at 1.8 Mrad caused no loss of potency nor change in any of the bacitracin components. Ethylene oxide treatment, on the other hand, caused considerable (46%) reduction of potency. Substantial reduction of areas under the peak of bacitracins A, B1, and B2 (50, 24 and 37%, respectively) were noted. The chromatograms showed numerous unresolved peaks around bacitracins A, B1 and B2,; however, no significant increase in the bacitracin F peak, nor appearance of non-UV absorbing peaks were observed. Peptide antibiotics of the polymyxin group, circulin, colistin, and polymyxin, were also analyzed using the muBondapak C18 column with a linear-gradient elution. A UV monitor was used for polymyxin. A moving-wire flame ionization detector was used to monitor circulin and colistin. A sample of polymyxin, circulin, and colistin may be analyzed in less than 20 min of chromatographic time.
|
| 237028 |
Purification and characterization of roseotoxin b, a toxic cyclodepsipeptide from Trichothecium roseum |
10.1021/jf60198a050. |
J Agric Food Chem |
Purification and characterization of roseotoxin b, a toxic cyclodepsipeptide from Trichothecium roseum
Abstract
|
| 266717 |
Amino acid sequence of human prothrombin fragments 1 and 2. |
10.1073/pnas.74.5.1969 |
Proc. Natl. Acad. Sci. U.S.A. |
Amino acid sequence of human prothrombin fragments 1 and 2.
Abstract
- The amino acid sequence of the nonthrombin half of human prothrombin is presented. Prothrombin fragment 1 has 155 amino acid residues as compared with 156 for the bovine equivalent. Ten gamma-carboxyglutamic acid residues are at the same location in each species. Human prothrombin fragment 2 contains 118 amino acid residues, as does the similar bovine fragment. Comparing bovine and human prothrombin fragment 1 we found 131 residues to be identical (84%). In prothrombin fragment 2, 84 residues were identical (71%). Assuming a time span of 90 million years since the radiation of several orders of placental mammals, prothrombin fragments 1 and 2 incorporated one substitution site per 100 amino acid sites every 11.2 and 6.3 million years, respectively. Internal homology is acribed to partial gene duplication, with the most likely crossover point located between residues 60-61 and residues 165-166.
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