Enhancement of antitumor activity of branchd β-1,3-glucans by chemical modification

1982 ◽  
Vol 4 (4) ◽  
pp. 266
Author(s):  
A. Misaki ◽  
T. Sasaki
1994 ◽  
Vol 41 (10) ◽  
pp. 733-740 ◽  
Author(s):  
Cun ZHUANG ◽  
Takashi MIZUNO ◽  
Hitoshi ITO ◽  
Keishiro SHIMURA

2004 ◽  
Vol 69 (11) ◽  
pp. 901-907 ◽  
Author(s):  
Dusan Sladic ◽  
Irena Novakovic ◽  
Zoran Vujcic ◽  
Tatjana Bozic ◽  
Natasa Bozic ◽  
...  

The avarone/avarol quinone/hydroquinone couple shows considerable antitumor activity. In this work, covalent modification of ?-lactoglobulin by avarone and its derivatives as well as by the synthetic steroidal quinone 2,5(10)-estradiene- 1,4,17-trione and its derivatives were studied. The techniques for studying chemical modification of ?-lactoglobulin by quinones were: UV/Vis spectrophotometry, SDS PAGE and isoelectrofocusing. SDS PAGE results suggest that polymerization of the protein occurs. It could be seen that the protein of 18 kD gives the bands of 20 kD, 36 kD, 40 kD, 45 kD, 64 kD and 128 kD depending on modification agent. The shift of the pI of the protein (5.4) upon modification toward lower values (from pI 5.0 to 5.3) indicated that lysine amino groups are the principal site of the reaction of ?-lactoglobulin with the quinones.


1983 ◽  
Vol 115 ◽  
pp. 199-208 ◽  
Author(s):  
Kazuhiro Inoue ◽  
Keiji Kawamoto ◽  
Hiroto Nakajima ◽  
Morihiro Kohno ◽  
Shizuo Kadoya ◽  
...  

1996 ◽  
Vol 60 (1) ◽  
pp. 30-33 ◽  
Author(s):  
Takashi Mizuno ◽  
Poohong Ykohlui ◽  
Tetsuya Kinoshita ◽  
Cun Zhuang ◽  
Hitoshi Ito ◽  
...  

2003 ◽  
Vol 68 (4-5) ◽  
pp. 243-248 ◽  
Author(s):  
Irena Novakovic ◽  
Zoran Vujcic ◽  
Tatjana Bozic ◽  
Natasa Bozic ◽  
Nenad Milosavic ◽  
...  

The avarone/avarol quinone/hydroquinone couple, as well as their derivatives show considerable antitumor activity. In this work, covalent modifications of ?-lactoglobulin, isolated from cow milk, by avarone, its model compound 2-tert-butyl-1,4-benzoquinone, and several of their alkylthio derivatives were studied. The techniques applied for assaying the modifications were UV/VIS spectrophotometry, SDS PAGE and isoelectrofocusing. The results of the SDS PAGE suggest that polymerisation of the protein occurs. The shift of the pI of the protein upon modification toward lower values indicates that lysine amino groups are the principal site of the reaction of ?-lactoglobulin with the quinines.


1985 ◽  
Vol 38 (7) ◽  
pp. 886-898 ◽  
Author(s):  
YOSHIHISA UMEDA ◽  
MAKOTO MORIGUCHI ◽  
HIROYUKI KURODA ◽  
TERUYA NAKAMURA ◽  
HIRONOBU IINUMA ◽  
...  

1984 ◽  
Vol 37 (10) ◽  
pp. 1264-1267 ◽  
Author(s):  
SATOSHI OMURA ◽  
KATSUJI MIYANO ◽  
AKIRA NAKAGAWA ◽  
HIROSHI SANO ◽  
KANKI KOMIYAMA ◽  
...  

1987 ◽  
Vol 40 (9) ◽  
pp. 1303-1315 ◽  
Author(s):  
YOSHIHISA UMEDA ◽  
MAKOTO MORIGUCHI ◽  
HIROYUKI KURODA ◽  
TERUYA NAKAMURA ◽  
AKIO FUJII ◽  
...  

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