RNase Digestion Mixture

2006 ◽  
Vol 2006 (1) ◽  
pp. pdb.rec401
Keyword(s):  
Digestion Mixture ◽  
Rnase Digestion

scholarly journals THE ESTIMATION OF ACTIVE NATIVE TRYPSIN IN THE PRESENCE OF INACTIVE DENATURED TRYPSIN

1933 ◽  
Vol 17 (2) ◽  
pp. 159-164 ◽  
Author(s):  
M. L. Anson ◽  
A. E. Mirsky
Keyword(s):  
Protein Solutions ◽  
Digestion Mixture ◽  
Tryptic Activity

Inactive denatured trypsin changes into active native trypsin in the protein solutions which have been used to estimate tryptic activity. If the digestion mixture, however, is alkaline enough and contains enough urea this change does not take place. Such a digestion mixture can be used to estimate active native trypsin in the presence of inactive denatured trypsin.

scholarly journals Rabbit globin mRNA: analysis of T1 RNAse digestion fragments.

1977 ◽  
Vol 252 (10) ◽  
pp. 3446-3458
Author(s):  
G V Paddock ◽  
R Poon ◽  
H C Heindell ◽  
J Isaacson ◽  
W Salser
Keyword(s):  
Globin Mrna ◽  
Rnase Digestion ◽  
Mrna Analysis

Induction of implantation in the rat by intraparametrial injection of uterine RNA from oestrogen-treated animals

1982 ◽  
Vol 93 (3) ◽  
pp. 397-NP ◽  
Author(s):  
B. Lejeune ◽  
F. Puissant ◽  
M. Camus ◽  
F. Leroy
Keyword(s):  
Messenger Rna ◽  
Rna Synthesis ◽  
Ovariectomized Rats ◽  
Pregnant Rats ◽  
Rnase Digestion

Crude RNA preparations from uteri of oestradiol-treated rats induced the implantation of delayed blastocysts when injected into the parametrium of ovariectomized pregnant rats. Treatment of donor animals with labelled oestradiol showed that this effect could not be due to contamination of the RNA extracts by oestradiol. RNase digestion of these extracts suppressed their capacity to induce implantation. Purified poly (A)-rich RNA from oestrogen-treated uteri failed to elicit implantation although it was capable of increasing epithelial height when repeatedly injected into uterine horns of ovariectomized rats. These results suggest that uterine RNA synthesis might somehow mediate the effects of oestrogen in causing implantation and that RNAs other than messenger RNA might be involved.

The Actions of Enzymes on Lampbrush Chromosomes

1962 ◽  
Vol s3-103 (62) ◽  
pp. 173-203
Author(s):  
H. C. MACGREGOR ◽  
H. G. CALLAN
Keyword(s):  
Proteolytic Enzymes ◽  
Lampbrush Chromosomes ◽  
Triturus Cristatus ◽  
Trichloracetic Acid ◽  
Protease Digestion ◽  
Lateral Loop ◽  
Peptic Digestion ◽  
Rnase Digestion ◽  
Break Chromosome ◽  
Loop Matrix

The chromomeres of lampbrush chromosomes of Triturus cristatus are Feulgen-positive; they therefore contain DNA. After removal of their DNA in boiling trichloracetic acid, the chromomeres stain with fast green at alkaline pH; they therefore contain basic protein. The lateral loops are Feulgen-negative; they stain with toluidine blue at acid pH, but much less intensely following RNase digestion; they therefore contain RNA. The spheres of chromosomes V and VIII do not contain RNA. Unfixed lampbrush chromosomes retain a life-like appearance in 0.07 M K/NaCl at pH 6.2; in this medium the nuclear sap disperses. As pH is raised to 8.5 the matrices of lateral loops dissolve but chromosome axes remain unbroken. Above pH 8.5 lampbrush chromosomes dissolve. As pH is lowered from 6.2, at between 5.8 and 5.4 coagulation occurs. If pH is rapidly reduced still further, a persistent relaxed condition sets in between 2.5 and 2. In concentrations of K/NaCl above 0.5 M lampbrush chromosomes dissolve. Lateral loop matrices dissolve in 0.25 M K/NaCl but chromosome axes remain unbroken. In concentrations of K/NaCl below 0.05 M lateral loop matrices dissolve, but even in distilled water chromosome axes remain unbroken. Trypsin at pH 6.2 and at pH 7.8 strips the matrices from lateral loops and occasionally breaks matrix fusions. It causes chromomeres to swell and coalesce, but fails to break chromosome axes. The action of ‘pan-protease’ resembles that of trypsin in all respects. Pepsin at pH 6.2 strips the matrices from lateral loops, but does not destroy chromomeres. At low pH peptic digestion is slow: the enzyme is attacking coagulated chromosomes; but if peptic digestion precedes a lowering of pH the overall outcome is a rapid solution of loop matrix, and under these conditions matrix and sphere fusions are broken. If trypsin or ‘pan-protease’ digestion precedes a lowering of pH there is a similarly rapid solution of loop matrix; thus the action is not specifically referable to pepsin. Under no conditions does pepsin break the axes of lampbrush chromosomes. RNase at pH 6.2 strips the matrices from lateral loops; this action is detectable at extreme dilution. RNase does not destroy chromomeres, nor does it break chromosome axes. If tryptic digestion follows RNase digestion this too fails to break chromosome axes. Unlike the proteolytic enzymes and RNase, DNase at pH 6.2 breaks the fibril between adjacent chromomeres, and it also breaks the axes of lateral loops. Contrary to Mazia's experience with salivary gland chromosomes, versene does not break the axes of lampbrush chromosomes even when applied in media of low electrolyte concentration. These results indicate that uninterrupted fibres of DNA run throughout the lengths of lampbrush chromosomes.

scholarly journals A unique ribonucleoprotein complex assembles preferentially on ecdysone-responsive sites in Drosophila melanogaster.

1993 ◽  
Vol 13 (9) ◽  
pp. 5323-5330 ◽  
Author(s):  
S A Amero ◽  
M J Matunis ◽  
E L Matunis ◽  
J W Hockensmith ◽  
G Raychaudhuri ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Polytene Chromosomes ◽  
Cell Extract ◽  
Sequence Motifs ◽  
Drosophila Cell ◽  
Rnase Digestion

The protein on ecdysone puffs (PEP) is associated preferentially with active ecdysone-inducible puffs on Drosophila polytene chromosomes and contains sequence motifs characteristic of transcription factors and RNA-binding proteins (S. A. Amero, S. C. R. Elgin, and A. L. Beyer, Genes Dev. 5:188-200, 1991). PEP is associated with RNA in vivo, as demonstrated here by the sensitivity of PEP-specific chromosomal immunostaining in situ to RNase digestion and by the immunopurification of PEP in Drosophila cell extract with heterogeneous nuclear ribonucleoprotein (hnRNP) complexes. As revealed by sequential immunostaining, PEP is found on a subset of chromosomal sites bound by the HRB (heterogeneous nuclear RNA-binding) proteins, which are basic Drosophila hnRNPs. These observations lead us to suggest that a unique, PEP-containing hnRNP complex assembles preferentially on the transcripts of ecdysone-regulated genes in Drosophila melanogaster presumably to expedite the transcription and/or processing of these transcripts.

Isolation and translation in vitro of poly(A)+ RNA from the free-living nematode Panagrellus silusiae

1979 ◽  
Vol 57 (4) ◽  
pp. 330-335 ◽  
Author(s):  
J. Scott Noble ◽  
J. Pasternak
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Mean Value ◽  
Amino Acid Incorporation ◽  
Free Living ◽  
Free Living Nematode ◽  
Rnase Digestion ◽  
Fold Stimulation ◽  
Cellulose Column

Polysomal RNA was isolated from the free-living nematode Panagrellus silusiae. Passage of this RNA through a cellulose column resulted in the fractionation of the input RNA into poly(A)− RNA (ca. 97.5% of the total) and poly(A)+ RNA (ca. 2.5% of the total). RNase digestion, followed by polyacrylamide gel electrophoresis, revealed that the poly(A)+ RNA contained poly(A) tracts that ranged from 75 to 104 nucleotides in length with a mean value of about 90 residues. There was no evidence of poly(A) sequences in the poly(A)− RNA fraction. Poly(A)+ RNA gave a 25- to 50-fold stimulation (over background) of amino acid incorporation in the wheat germ cell-free protein-synthesizing system. At least 26 proteins were evident after electrophoresis in cylindrical sodium dodecyl sulfate – polyacrylamide gels. Poly(A)− RNA was capable of stimulating protein synthesis in vitro with about five discrete proteins being produced. In summary, the properties of mRNA from a simple organism such as P. silusiae are very similar to those of more complex eukaryotes.

RNase Digestion Buffer

2013 ◽  
Vol 2013 (3) ◽  
pp. pdb.rec074146
Keyword(s):  
Rnase Digestion

Casein Kinase 2 and Protein Substrates Are Released from Rat Liver Cells Nuclei by DNAse or RNase Digestion

1994 ◽  
Vol 202 (2) ◽  
pp. 984-991 ◽  
Author(s):  
R. Bosser ◽  
J. Roig ◽  
E. Itarte ◽  
O. Bachs
Keyword(s):  
Rat Liver ◽  
Liver Cells ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Protein Substrates ◽  
Rat Liver Cells ◽  
Rnase Digestion

scholarly journals A Set of Novel RNAs Transcribed from the Chloroplast Genome Accumulates in Date Palm Leaflets Affected by Brittle Leaf Disease

2008 ◽  
Vol 98 (3) ◽  
pp. 337-344 ◽  
Author(s):  
J. Marqués ◽  
Z. G. N. Fadda ◽  
N. Duran-Vila ◽  
R. Flores ◽  
J. M. Bové ◽  
...  
Keyword(s):  
Chloroplast Genome ◽  
Date Palm ◽  
Diagnostic Value ◽  
Northern Hybridization ◽  
Date Palms ◽  
Leaf Disease ◽  
Southern Tunisia ◽  
Rnase Digestion

Brittle leaf disease or maladie des feuilles cassantes (MFC) is a lethal disorder of date palms that has assumed epidemic proportions in the oases of southern Tunisia. After a prolonged period during which palms are declining, the disease ends with the death of the palms. Whereas no pathogen could ever be associated with the disease, leaflets of affected palms have been previously shown to be deficient in manganese. Analysis of RNA preparations from leaflets of MFC-affected palms revealed the presence of a set of novel RNAs (MFC-RNAs) of sense and antisense polarities, which are homologous to various regions of the date palm chloroplast genome, such as the regions containing genes rrn5S-trnR(ACG) and trnM(CAU)-atpE. In the RNA preparations obtained from leaflets of affected palms, some of these RNAs are present as double-stranded species (MFC-dsRNAs), as witnessed by results from cellulose chromatography, end labeling, RNase digestion, and northern hybridization with strand specific probes. These MFC-RNAs represent a novel type of host-derived RNAs, and their presence in MFC-affected date palms is of diagnostic value.

Digestion of Sugar Beet Leaves for Atomic Absorption Spectroscopy

1969 ◽  
Vol 23 (4) ◽  
pp. 354-357 ◽  
Author(s):  
Merle Harrison ◽  
Charles Andre
Keyword(s):  
Sugar Beet ◽  
Atomic Absorption ◽  
Absorption Spectroscopy ◽  
Atomic Absorption Spectroscopy ◽  
Sodium Molybdate ◽  
Plant Materials ◽  
Digestion Mixture ◽  
Interfering Ions

A modified digestion mixture utilizing sodium molybdate as a catalyst is described for plant materials. In atomic absorption spectroscopy, special attention is given to calcium analyses using this mixture, because of various interfering ions. The digestion mixture is suitable for numerous other cation determinations. Also, a method of increasing the sensitivity for copper by adding methanol is described.

Sign in / Sign up

Export Citation Format

Share Document