scholarly journals Number and activity of active ribosomes in bacterial polyribosomes

1977 ◽  
Vol 164 (3) ◽  
pp. 669-674 ◽  
Author(s):  
J Stenesh ◽  
P Y Shen
Keyword(s):  
Amino Acid ◽  
Bacillus Stearothermophilus ◽  
Polypeptide Chains ◽  
Active Ribosome

Polyribosomes were isolated from Baccillus licheniformis, grown at 37 and 46 degrees C, and from Bacillus stearothermophilus, grown at 46 and 55 degrees C. The polyribosomes were incubated with either [3H]puromycin or [14C]phenylalanine. The number of active ribosomes (i.e. those to which growing polypeptide chains are attached) was calculated from the amount of [3H]peptidyl-puromycin formed. The activity of an active ribosome (i.e. the total number of amino acid molecules incorporated/unit time per active ribosome) was calculated from the uptake of [14C]phenylalanine. The number of active ribosomes per migrogram of RNA was as follows: for B. licheniformis, 1.66 × 10(12) and 1.72 × 10(12) at 37 and 46 degrees C respectively; for B. stearothermophilus, 2.59 × 10(12) at 46 and 55 degreesC respectively. The activity per active ribosome was as follows: for B. licheniformis, 0.61 and 0.05 at 37 and 46 degrees C respectively; for B. stearothermophilus, 0.58 and 0.42 at 46 and 55 degrees C respectively.

Amino-Acid Sequence of the αD- and ß-Polypeptide Chains of the Japanese Quail Hemoglobin

1993 ◽  
Vol 374 (1-6) ◽  
pp. 111-116 ◽  
Author(s):  
Yukinori EGUCHI ◽  
Yasutugu NAKASHIMA ◽  
Hiroshi TAKEI
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Japanese Quail ◽  
Polypeptide Chains

SOME ASPECTS OF THE STRUCTURE OF HEMOGLOBIN

1964 ◽  
Vol 42 (6) ◽  
pp. 755-762 ◽  
Author(s):  
David B. Smith
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Partial Amino Acid Sequence ◽  
Heme Pocket ◽  
Terminal Amino ◽  
Polypeptide Chains ◽  
Kinetics Of ◽  
Β Chain

An outline of present ideas concerning the arrangement, folding, and chemistry of the polypeptide chains of hemoglobin is given with some references to present know ledge of myoglobin.New material includes a partial amino acid sequence of the β-chain of horse hemoglobin, details concerning the amino acids lining the heme pocket of horse hemoglobin, and the effects of carboxypeptidases A and B on horse oxy- and horse deoxy-hemoglobin. The kinetics of the latter reactions are not simple. The C-terminal amino acids are released more rapidly from the oxygenated form.

Existence of Common Antigenic Determinants in the Aα, Bβ and γ Chains of Some Mammalian Fibrinogens.

1979 ◽  
Author(s):  
C.S. Cierniewski
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Antigenic Determinants ◽  
Terminal Amino Acid ◽  
Human Fibrinogen ◽  
Passive Hemagglutination ◽  
Terminal Amino ◽  
Polypeptide Chains ◽  
Fibrinogen Molecule

Polypeptide chains Aα, Bβ and γ of porcine fibrinogen were isolated by preparative SDS polyacrylamide gel electrophoresis. Their purity was estimated by electrophoresis in polyacrylamide gel, amino acid composition and N-terminal amino acid analyses. Antisera to the pig polypeptide chains were produced in rabbits and they were employed in immunological comparative studies of porcine, bovine, human and duck fibrinogens. Antisera to the pig Aα chain showed in gel immunodiffusion and passive hemagglutination a strong cross-reaction with porcine, bovine and human fibrinogens. Antisera to the pig βB and γ chains cross-reacted only with porcine and bovine fibrinogens but they did not recognize human fibrinogen, The reaction of antiγ antisera was detectable only by passive hemagglutination test. In all cases antigenic similarity of the analyzed fibrinogens was mainly related to antigenic determinants of the Aα, Bβ and γ chains exposed on the intact fibrinogen molecule. None of analyzed antisera reacted with duck fibrinogen.

scholarly journals Biochemical characterization of a second family of human Ia molecules, HLA-DS, equivalent to murine I-A subregion molecules.

1982 ◽  
Vol 156 (2) ◽  
pp. 550-566 ◽  
Author(s):  
S M Goyert ◽  
J E Shively ◽  
J Silver
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequence Identity ◽  
Biochemical Characterization ◽  
Amino Acid Sequence Homology ◽  
Molecular Weights ◽  
Hla Dr ◽  
D Region ◽  
Polypeptide Chains

In mice, two families of structurally distinct Ia molecules, one designated I-A and the other I-E, have been identified and characterized. The HLA-DR molecules represent one family of human Ia molecules equivalent to the murine I-E molecules on the basis of amino acid sequence homology. We describe the isolation and biochemical characterization of a second family of human Ia molecules, designated HLA-DS for second D-region locus, equivalent to the murine I-A molecules. The human HLA-DS molecules consist of two polypeptide chains, DS alpha (37,000 mol wt) and DS beta (29,000 mol wt), with 73% amino acid sequence identity to the murine I-A molecules. Furthermore, the HLA-DS molecules are closely linked genetically to HLA-DR molecules, a situation analogous to that observed in mice. The similarity in molecular weights of the DR and DS molecules might explain why others have failed to identify the latter in man.

scholarly journals Partial Chemical Characterization of S-Carboxymethylated Chains of Rabbit Fibrin(OGEN): Evidence for Separate Chain Biosynthesis

1977 ◽  
Author(s):  
B. Alving ◽  
G. Murano ◽  
D. Walz
Keyword(s):  
Amino Acid ◽  
Specific Activity ◽  
Chemical Characterization ◽  
Molecular Size ◽  
Exchange Chromatography ◽  
12 Steps ◽  
Polypeptide Chains ◽  
Sds Electrophoresis ◽  
Derivatives Of

The purpose of this study was twofold: 1) chemically characterize the isolated polypeptide chains of rabbit fibrin(ogen), and 2) explore their mode of biosynthesis. The three S-carboxy-methyl polypeptide chain derivatives of rabbit fibrin (α, β and γ) were isolated by cation exchange chromatography. Their amino acid composition was similar to the human with a methionine distribution (mole/mole) as follows: γ = 9; β = 14, α = 14. Their molecular size, (SDS electrophoresis) was estimated as follows: γ = 46,000; β = 54,000; α = 63,500. The N-terminal amino acid sequence (12 steps) of the β derivative was:Gly-His-Arg-Pro-Ile-Asp-Arg-Arg-Arg-Glu-Glu-Leu-. To determine whether the three chains are synthesized sequentially (one continuous chain, later split into three) or in parallel, turpentine-stimulated male New Zealand rabbits were given ~40 μCi of [75Se] selenomethionine (SeM) and its incorporation into fibrinogen (F) was followed. F was clotted from plasma samples, washed, reduced, and constituent chains separated by gel electrophoresis in the presence of SDS-urea. The radioactivity of each chain (expressed as percent of total F radioactivity) was determined, and the specific methionine radioactivity calculated for each chain isolated at 20, 25, and 30 min after SeM injection. During this interval the specific activity of the α and the γ chains was essentially the same (within 3%) while that of the β chain was 42 to 97% greater than that of the α chain. The similar activity of the α and γ chains during the early phase of SeM incorporation suggests that these two chains are not synthesized sequentially, rather they are synthesized in parallel.

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