scholarly journals Chemical modification of amino groups in alanine dehydrogenase from Bacillus natto KMD 1126.

1981 ◽  
Vol 29 (2) ◽  
pp. 485-489 ◽  
Author(s):  
KATSUHIKO MATSUI ◽  
KIYOMI FUKUDA ◽  
YUKIO KAMEDA
Keyword(s):  
Chemical Modification ◽  
Amino Groups ◽  
Bacillus Natto ◽  
Alanine Dehydrogenase

scholarly journals Chemical modification of the adeno-associated virus capsid to improve gene delivery

2020 ◽  
Vol 11 (4) ◽  
pp. 1122-1131 ◽  
Author(s):  
Mathieu Mével ◽  
Mohammed Bouzelha ◽  
Aurélien Leray ◽  
Simon Pacouret ◽  
Mickael Guilbaud ◽  
...  
Keyword(s):  
Gene Delivery ◽  
Chemical Modification ◽  
Neutralizing Antibodies ◽  
Cell Tropism ◽  
Amino Groups ◽  
Chemical Modifications ◽  
Virus Capsid ◽  
Adeno Associated Virus

Bioconjugated AAV vectors, achieved by coupling of ligands on amino groups of the capsid, are of great interest for gene delivery. Chemical modifications can be used to enhance cell tropism and to decrease interactions with neutralizing antibodies.

Chemical Modification of the Hemolytic Lectin CEL-III by Succinic Anhydride: Involvement of Amino Groups in the Oligomerization Process

1998 ◽  
Vol 62 (6) ◽  
pp. 1185-1189 ◽  
Author(s):  
Tomomitsu HATAKEYAMA ◽  
Yumiko MATSUYAMA ◽  
Takako FUNADA ◽  
Sachiko FUKUYAMA ◽  
Hiromiki KUWAHARA ◽  
...  
Keyword(s):  
Chemical Modification ◽  
Succinic Anhydride ◽  
Amino Groups

scholarly journals Purification and properties of alanine dehydrogenase from Bacillus natto KMD 1126.

1977 ◽  
Vol 25 (8) ◽  
pp. 2061-2066 ◽  
Author(s):  
KATSUHIKO MATSUI ◽  
YUKIKO TAMEGAI ◽  
AKIKO MIYANO ◽  
YUKIO KAMEDA
Keyword(s):  
Bacillus Natto ◽  
Alanine Dehydrogenase ◽  
Purification And Properties

scholarly journals Protein covalent modification of biologically active quinones

2004 ◽  
Vol 69 (11) ◽  
pp. 901-907 ◽  
Author(s):  
Dusan Sladic ◽  
Irena Novakovic ◽  
Zoran Vujcic ◽  
Tatjana Bozic ◽  
Natasa Bozic ◽  
...  
Keyword(s):  
Antitumor Activity ◽  
Chemical Modification ◽  
Covalent Modification ◽  
Biologically Active ◽  
Amino Groups ◽  
Sds Page ◽  
Protein Covalent

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.

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