scholarly journals The presence of ribonucleic acid in the cell walls of higher plants

1968 ◽  
Vol 108 (1) ◽  
pp. 25-31 ◽  
Author(s):  
P. D. Phethean ◽  
L. Jervis ◽  
Mary Hallaway

A method for isolating extensively purified cell walls from higher plants is described; the preparations contain no detectable chloroplast or nuclear material and the protein content (2–5% of the dry wt. of walls) indicates that there is little contamination with cytoplasm. Incubation of purified cell walls with 0·3n-potassium hydroxide for 17hr. at 37° liberates ribonucleotides, which can be purified by adsorption on charcoal and by ion-exchange chromatography. Ribonucleotides are also liberated by incubating the walls with ribonuclease, but not with deoxyribonuclease. The RNA content varies from 0·5 to 6mg./g. dry wt. of walls, depending on the nature and age of the tissue, and at 3mg./g. dry wt. of walls accounts for about 7% of the total RNA of the tissue. Less than 0·2% of the RNA of the walls is due to the presence of bacteria in the preparation. The base composition of the cell-wall RNA is identical with that of ribosomal RNA.

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.


2018 ◽  
Vol 20 (1) ◽  
pp. 56-60 ◽  
Author(s):  
Tsutomu Arakawa

Proteins often generate structure isoforms naturally or artificially due to, for example, different glycosylation, disulfide scrambling, partial structure rearrangement, oligomer formation or chemical modification. The isoform formations are normally accompanied by alterations in charged state or hydrophobicity. Thus, isoforms can be fractionated by reverse-phase, hydrophobic interaction or ion exchange chromatography. We have applied mixed-mode chromatography for fractionation of isoforms for several model proteins and observed that cation exchange Capto MMC and anion exchange Capto adhere columns are effective in separating conformational isoforms and self-associated oligomers.


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