The differentiation of α- and β -glucosidase and α- and β-galactosidase isoenzymes from maize and broad bean root tips using disc electrophoresis in polyacrylamide gels

1977 ◽  
Vol 19 (6) ◽  
pp. 436-441 ◽  
Author(s):  
VĚra HadačOvá ◽  
K. Bbeneš
1988 ◽  
Vol 30 (4) ◽  
pp. 300-304
Author(s):  
Dagmar TomÁškovÁ ◽  
K. Beneš ◽  
A. Holô

1970 ◽  
Vol 23 (3) ◽  
pp. 573 ◽  
Author(s):  
RJ Rose

Cycloheximide blocked cell division at interphase, prophase, prometaphase, metaphase, and telophase in Jerusalem artichoke tuber tissue. Blocking at anaphase did not occur or was very infrequent. In any cell, the location of the block depended upon the stage of the cell cycle reached at the time of cycloheximide addition. In general, cycloheximide caused similar blocks in interphase and mitosis in cells of synchronised broad bean root tips. A reduction of mitotic frequency occurred after about 8 hr in cycloheximide, indicating a reversion of chromosome coiling.


1975 ◽  
Vol 30 (11-12) ◽  
pp. 781-784 ◽  
Author(s):  
E. Jürgen Zöllner ◽  
Hans Störger ◽  
Hans-Joachim Breter ◽  
Rudolf Zahn

Abstract Deoxyribonucleases, Disc Electrophoresis, Lymphocytes Four groups of deoxyribonuclease activities from human lymphocytes have been characterized by deoxyribonuclease assay in DNA-containing polyacrylamide gels following their separation by disc-electrophoresis. All activities hydrolyse DNA endonucleolytically. One neutral deoxyribo­ nuclease found in the cytoplasmic fraction prefers native or UV-irradiated DNA over denatured DNA as substrate and is a 5′-monoester former. Two groups of acid deoxyribonuclease activities are detectable in the nuclear fraction. Both are 3′-monoester formers. One is as well active with denatured DNA as with native DNA, the other one shows the same activity with native and UV-irradiated DNA but lower activity with denatured DNA. An alkaline deoxyribonuclease activity, also localized in the nucleus, is a 5′ -monoester DNA as substrate.


PROTOPLASMA ◽  
2012 ◽  
Vol 250 (2) ◽  
pp. 531-538 ◽  
Author(s):  
Valeriya Krylova ◽  
Igor M. Andreev ◽  
Rozaliya Zartdinova ◽  
Stanislav F. Izmailov

Plant Science ◽  
2005 ◽  
Vol 168 (4) ◽  
pp. 1005-1010 ◽  
Author(s):  
Igor Andreev ◽  
Valeria Krylova ◽  
Pavel Dubrovo ◽  
Stanislav Izmailov

1973 ◽  
Vol 51 (11) ◽  
pp. 2217-2222 ◽  
Author(s):  
R. B. van Huystee

The prime purpose of this proteolysis study was to direct attention to alternate means of measuring proteolytic activity other than the determination of free amino acids. The release of peptides from a macromolecular protein during incubation with either papain, pronase, or trypsin was determined by measuring the presence of 280-nm-absorbing molecules in the fractionation range of Sephadex G 25 eluant after incubation. The formation of larger proteinaceous constituents by proteolysis of arachin was analyzed by disc electrophoresis on polyacrylamide gels. Using these techniques it was noted that papain was the most efficient proteolytic agent for the degradation of arachin.


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