Analysis of the surface structures of the sea urchin egg by means of antibodies. II. The J- and A-antigens |
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| Authors: | PERLMANN P PERLMANN H |
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| Affiliation: | 1. The Swire Institute of Marine Science, School of Biological Sciences, The University of Hong Kong, Hong Kong, China;2. Key Laboratory of Mariculture, Ministry of Education, Ocean University of China, Qingdao, 266003, China;3. Shandong Provincial Key Laboratory of Animal Biotechnology and Disease Control and Prevention, Shandong Agricultural University, Taian City, 271018, China;4. Laboratory for Marine Fisheries Science and Food Production Processes, Qingdao National Laboratory for Marine Science and Technology, Qingdao, 266237, China;1. School of Marine Sciences, Ningbo University, Ningbo, Zhejiang Province, 315211, PR China;2. Key Laboratory of Mariculture & Stock Enhancement in North China''s Sea, Ministry of Agriculture and Rural Affairs, Dalian Ocean University, Dalian, 116023, PR China;1. Auburn University, Department of Biological Sciences, Auburn, AL, 36830, USA;2. University of Nebraska - Lincoln, Department of Biological Systems Engineering, Lincoln, NE 68588, USA;3. Texas A&M University, Department of Biology, College Station, TX 77843, USA |
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| Abstract: | In the course of an immunochemical investigation of the surface layers of the sea urchin egg, the jelly-precipitating and the parthenogenetic actions of rabbit antiserum on the eggs of Paracentrotus lividus were studied by means of antiserum inhibition techniques. - 1.1. The jelly precipitation, obtained with antiserum, is due to the reaction between antibodies and a particular antigen of the egg jelly, the J-antigen. The J-antigen is heat stable at pH 7 to 8. It is destroyed when heated to 100 °C at pH 1. It is also susceptible to oxidation with periodate and heating to 100 °C at pH 3.5. The J-antigen is an integral part of the main polysaccharide of the jelly layer.
- 2.2. The parthenogenetic activation of the egg by means of antiserum is due to the reactions between antibodies and a particular antigen, the A-antigen. The A-antigen does not belong to the egg proteins destroyed by the action of trypsin and pepsin. It is soluble and heat stable at pH 7 to 8. It is destroyed when heated to 100 °C at pH 1 and is also susceptible to periodate. Thus, the A-antigenic determinants are assumed to have a polysaccharide nature.
- 3.3. The A-antigen and the J-antigen are immunologically different molecules. The A-antigen belongs to the egg but it may also occur in the jelly layer. It is assumed that the A-antigen constitutes a part of the cytoplasmic egg surface. There is some evidence which indicates that the A-antigenic principles belong to a molecule, containing glucose and sulfate.
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