Immunochemical relationship between glucoamylases I and II ofAspergillus niger

1980 ◽  
Vol 2 (3) ◽  
pp. 163-169 ◽  
Author(s):  
P. Manjunath ◽  
M. R. Raghavendra Rao
Keyword(s):  
Immunochemical Relationship

scholarly journals Studies on the Mitotic Apparatus of the Sea Urchin by Means of Antigen-Antibody Reactions in Agar

1959 ◽  
Vol 6 (3) ◽  
pp. 447-455 ◽  
Author(s):  
Hans A. Went
Keyword(s):  
Sea Urchin ◽  
Strongylocentrotus Purpuratus ◽  
Structural Elements ◽  
Agar Gel ◽  
Mitotic Apparatus ◽  
Insoluble Form ◽  
Molecular Origin ◽  
Antigen Antibody ◽  
Gel Diffusion ◽  
Immunochemical Relationship

The primary purpose of the experiments reported in this paper was to gain information on the molecular origin of the mitotic apparatus. Antisera were prepared against unfertilized sea urchin (Strongylocentrotus purpuratus) egg antigens and mitotic apparatus antigens. These were permitted to react with various antigen solutions in Ouchterlony agar gel diffusion plates, and the resultant precipitation patterns analysed. The results revealed that the mitotic apparatus contains probably no more than two antigens (precursor-1 component and precursor-2 component) and that these are shared by the unfertilized egg. Absorption and fractionation techniques indicated that in the unfertilized egg the precursor-1 component is present both as a "soluble" protein and as an insoluble form tenaciously associated with intracellular structural elements. A survey of dividing and non-dividing tissues for the precursor-1 component revealed that it was restricted to tissues in which mitotic activity could be detected microscopically. No immunochemical relationship could be detected between the mitotic apparatus and proteins extracted, by various methods, from the lantern muscle.

Immunochemical Relationship Between Forssman and Globoside Glycolipid Antigens

1981 ◽  
Vol 10 (3) ◽  
pp. 237-250 ◽  
Author(s):  
R. A. Karol ◽  
S. K. Kundu ◽  
D. M. Marcus
Keyword(s):  
Immunochemical Relationship

Structural and immunochemical relationship between the O-antigenic polysaccharides from the enteroaggregative Escherichia coli strain 396/C-1 and Escherichia coli O126

2004 ◽  
Vol 339 (8) ◽  
pp. 1491-1496 ◽  
Author(s):  
E.Andreas Larsson ◽  
Felipe Urbina ◽  
Zhennai Yang ◽  
Andrej Weintraub ◽  
Göran Widmalm
Keyword(s):  
Escherichia Coli ◽  
Coli Strain ◽  
Immunochemical Relationship

scholarly journals Immunochemical relationship between α-amylases of rat liver, serum, pancreas and parotid gland

1975 ◽  
Vol 151 (1) ◽  
pp. 17-22 ◽  
Author(s):  
M Messer ◽  
R T Dean
Keyword(s):  
Parotid Gland ◽  
Rat Liver ◽  
Serum Amylase ◽  
Pancreatic Amylase ◽  
Rat Parotid Gland ◽  
Rat Parotid ◽  
Immunochemical Relationship

1. Rabbit antisera to purified rat parotid α-amylase were prepared. 2. The relationships between rat parotid-gland, pancreatic, serum and liver amylase were investigated by using the antisera in immunodiffusion, immunoelectrophoresis and immunoinhibition experiments. 3. Serum and liver amylase were identical, and very similar to parotid-gland amylase; pancreatic amylase was, however, quite distinct, and showed only some of the determinants present on parotid-gland amylase. 4. The data strengthen the suggestion that the liver is the main source of serum amylase.

Immunochemical relationship of d-amino acid oxidases in various tissues and animals

1991 ◽  
Vol 99 (2) ◽  
pp. 345-350 ◽  
Author(s):  
Masanao Katagiri ◽  
Hiromasa Tojo ◽  
Kihachiro Horiike ◽  
Toshio Yamano
Keyword(s):  
Amino Acid ◽  
Relationship Of ◽  
Immunochemical Relationship

Immunochemical Relationship of Human Plasma Beta-Lipoprotein and Chylomicrons

1956 ◽  
Vol 185 (2) ◽  
pp. 309-312 ◽  
Author(s):  
Elliott Middleton
Keyword(s):  
Human Serum Albumin ◽  
Human Plasma ◽  
Rabbit Serum ◽  
Low Density ◽  
Agar Gel ◽  
Absorption Studies ◽  
Relationship Of ◽  
Hydrolysis Of ◽  
Gel Diffusion ◽  
Immunochemical Relationship

Sf 3–8 human plasma beta-lipoprotein was prepared in the ultracentrifuge and was shown to be electrophoretically and ultracentrifugally homogeneous. Studies of this material with rabbit antisera to it indicated marked immunological inhomogeneity by agar gel diffusion and supernatant tests. Saline washed human chylomicrons reacted with the anti-beta-lipoprotein sera only after steapsin hydrolysis of the chylomicrons. No reaction between washed hydrolyzed chylomicrons and anti-human-serum-albumin rabbit serum was noted. Serial absorption studies indicated that chylomicrons and Sf 3–8 beta-lipoprotein are not immunologically identical but in the low density chylomicron fraction there is some substance antigenically related to Sf 3–8 beta-lipoprotein.

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