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Biomedical subjects

K Toczko

Publications and source records attributed to K Toczko.

At least 37 records · Page 2Linked to original sources

Nucleoprotein chromatin subunit from Physarum polycephalum.

The nucleoproteins resulting from digestion of the nuclei of the true slime mold Pysarum polycephalum with micrococcal nuclease have been resolved according to the size classes in linear sucrose gradients containg 0.5 M NaCl, and analysed for DNA, RNA and protein content. The basic nucleoprotein subunit has been found to contain a DNA fragment of about 150--170 base pairs complexed with an approximately equal amount, on a weight basis, of basic proteins and a relatively small amount of non-histone proteins (about 35% of the amount of DNA). Higher nucleoprotein oligomers were shown to contain spacer DNA fragments between adjacent subunits and a considerably higher ratio of non-histone proteins to DNA than the basic subunit. Both the basic subunit and higher nucleoprotein oligomers of Physarum chromatin contain some amount of tightly bound RNA. However, in contrast to the distribution of the non-histone proteins, the ratio of RNA to RNA is similar in both fractions.

Chromatin↗

The presence of serine protease in pea embryo chromatin.

1. It has been shown that chromatin from pea seedlings contains a proteolytic enzyme, similar to that of mammalian chromatin. 2. The protease was isolated from chromatin by acid extraction and partly characterized. It is a serine-type enzyme, sensitive to DFP, of low mol. wt. (about 18 000 - 20 000), with optimum pH at about 8 with [3H]N-acetylated histone as a substrate. 3. In chromatin complex, histones fl and f3 are preferentially degraded.

Chromatin↗

Changes in size and shape of chromatin particles after successive removal of histones.

The preparations of whole chromatin, chromatin selectively depleted of histone f1, depleted of all lysine-rich histones (f1, f2b, f2a2), and DNA was studied by viscosimetric and light scattering methods. The obtained results were used for calculation of the dimensions and packing ratios of DNA for the preparations studied. The packing ratio in whole chromatin is 7.2 and is almost unaffected by selective removal of histone f1 (6.9), but decreases on successive removal of the remaining four histones, the decrease being dependent more on the quantity than the kind of the dissociated histones.

Animals↗

Similarity in active site arrangement of neutral protease from calf thymus chromatin and trypsin.

1. Susceptibility to inhibitors of neutral protease from calf thymus chromatin has been compared with that of trypsin. The chromatin protease reacts stoichiometrically with the inhibitors specific for trypsin (diisopropylfluorophosphate, tosyl-lysyl chloromethane, soybean trypsin inhibitor and Kunitz basic inhibitor from pancreas), but not with the inhibitor specific for chymotrypsin (tosyl-phenylalanyl chloromethane). 2. Chromatin protease, similarly as trypsin, cleaves Lys-X and Arg-X peptide bonds. 3. It is concluded that the structure of active site region of both enzymes is very similar.

Animals↗

On the arrangement of histones in chromatin.

It was found that nucleoprotein particles formed after DNase I action on calf thymus chromatin contain single-stranded DNA fragments, associated with histones only by ionic linkages. These results suggest that histones in chromatin are bound ionically only to one polynucleotide strand of double-helical DNA, protecting it against nucleolytic attack.

Chromatin↗