Transcriptional reactivation of isolated Xenopus erythrocyte nuclei: patterns of RNA synthesis

1977 ◽  
Vol 28 (1) ◽  
pp. 49-60
Author(s):  
S.P. Gregory ◽  
V.A. Hilder ◽  
N. Maclean
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Rna Synthesis ◽  
Gene Activity ◽  
Low Molecular Weight ◽  
Isolated Nuclei ◽  
Cytoplasmic Proteins ◽  
Competitive Hybridization ◽  
Transcriptional Reactivation

Nuclei isolated from Xenopus erythrocytes can be transcriptionally reactivated by exposure to certain cytoplasmic proteins. The types of RNA synthesized during this reactivation have been studied and compared with those present in, or synthesized by, isolated nuclei not so reactivated or in entire Xenopus erythrocytes. In all cases, the pattern of transcription indicates the synthesis of a broad range of low molecular weight RNAs. Competitive hybridization demonstrates that the reactivated nuclei synthesize some transcripts not normally produced by the isolated nuclei and we have shown that a proportion of these possess amino acid-accepting activity. The significance of these results is discussed in relation to the control of gene activity in these cells.

scholarly journals The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase

1989 ◽  
Vol 264 (5) ◽  
pp. 2560-2567
Author(s):  
G Camici ◽  
G Manao ◽  
G Cappugi ◽  
A Modesti ◽  
M Stefani ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Acid Phosphatase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Low Molecular Weight ◽  
Complete Amino Acid Sequence

scholarly journals Characterization of Trypsin Inhibitor in Florunner Peanut Seeds (Arachis hypogaea L.)1

1988 ◽  
Vol 15 (2) ◽  
pp. 81-84 ◽  
Author(s):  
E. M. Ahmed ◽  
J. A. Applewhite
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Aspartic Acid ◽  
Arachis Hypogaea ◽  
Trypsin Inhibitor ◽  
Low Molecular Weight ◽  
Arachis Hypogaea L ◽  
Amino Acid Profiles ◽  
Low Levels

Abstract Florunner peanut seeds contained five trypsin isoinhibitors. Amino acid profiles of the trypsin inhibitors fraction showed high levels of aspartic acid, half-cystine and serine and low levels of histidine and tyrosine. The molecular weight of the inhibitor was 8.3 KDa. The presence of multiforms of this inhibitor, its low molecular weight and the high amount of half-cystine indicate that peanut trypsin inhibitor is of the Bowman-Birk type.

Normal Mature Human Enamel Protein

1979 ◽  
Vol 58 (2_suppl) ◽  
pp. 986-987 ◽  
Author(s):  
A. Belcourt
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Gel Electrophoresis ◽  
Protein Concentration ◽  
Polyacrylamide Gel Electrophoresis ◽  
Organic Matrix ◽  
Low Molecular Weight ◽  
Human Enamel ◽  
Weak Density ◽  
Enamel Protein

Pure enamel was prepared using an original microdissection technic. Protein concentration was 375 μg per gram of enamel. Polyacrylamide gel electrophoresis showed a single fast-migrating zone containing a thin double band. Ultracentrifugation studies suggested that the proteins were of low molecular weight or of weak density. Absorption spectra showed a strong absorbance at 260nm. Amino acid analyses yielded a composition of 25% Gly, 13.5% Glu, 11% Ser, 11% Pro, 2% Cys and 2% Hyp. A glucidic content of 15% was estimated and glucose, galactose, mannose and fucose were identified. The organic matrix of enamel seemed to be constituted of two major glycoproteins probably fibrous but different from keratin.

A Favorable, Narrow, δh Hansen-Parameter Domain for Gelation of Low-Molecular-Weight Amino Acid Derivatives

2011 ◽  
Vol 17 (48) ◽  
pp. 13603-13612 ◽  
Author(s):  
Pasquale Curcio ◽  
Florent Allix ◽  
Guillaume Pickaert ◽  
Brigitte Jamart-Grégoire
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Derivatives ◽  
Low Molecular Weight ◽  
Parameter Domain

Using a Genetically Encoded Fluorescent Amino Acid as a Site-Specific Probe to Detect Binding of Low-Molecular-Weight Compounds

2011 ◽  
Vol 9 (1) ◽  
pp. 50-57 ◽  
Author(s):  
Isaac N. Ugwumba ◽  
Kiyoshi Ozawa ◽  
Laura de la Cruz ◽  
Zhi-Qiang Xu ◽  
Anthony J. Herlt ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Low Molecular Weight ◽  
Specific Probe ◽  
Site Specific ◽  
Low Molecular Weight Compounds ◽  
Fluorescent Amino Acid ◽  
A Site

scholarly journals Genes for low-molecular-weight heat shock proteins of soybeans: sequence analysis of a multigene family.

1985 ◽  
Vol 5 (12) ◽  
pp. 3417-3428 ◽  
Author(s):  
R T Nagao ◽  
E Czarnecka ◽  
W B Gurley ◽  
F Schöffl ◽  
J L Key
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Heat Shock ◽  
Dna Sequences ◽  
Regulatory Element ◽  
Amino Acid Sequences ◽  
Striking Similarity ◽  
Low Molecular Weight ◽  
Genes Encoding ◽  
Flanking Regions

Soybeans, Glycine max, synthesize a family of low-molecular-weight heat shock (HS) proteins in response to HS. The DNA sequences of two genes encoding 17.5- and 17.6-kilodalton HS proteins were determined. Nuclease S1 mapping of the corresponding mRNA indicated multiple start termini at the 5' end and multiple stop termini at the 3' end. These two genes were compared with two other soybean HS genes of similar size. A comparison among the 5' flanking regions encompassing the presumptive HS promoter of the soybean HS-protein genes demonstrated this region to be extremely homologous. Analysis of the DNA sequences in the 5' flanking regions of the soybean genes with the corresponding regions of Drosophila melanogaster HS-protein genes revealed striking similarity between plants and animals in the presumptive promoter structure of thermoinducible genes. Sequences related to the Drosophila HS consensus regulatory element were found 57 to 62 base pairs 5' to the start of transcription in addition to secondary HS consensus elements located further upstream. Comparative analysis of the deduced amino acid sequences of four soybean HS proteins illustrated that these proteins were greater than 90% homologous. Comparison of the amino acid sequence for soybean HS proteins with other organisms showed much lower homology (less than 20%). Hydropathy profiles for Drosophila, Xenopus, Caenorhabditis elegans, and G. max HS proteins showed a similarity of major hydrophilic and hydrophobic regions, which suggests conservation of functional domains for these proteins among widely dispersed organisms.

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