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IMMUNITY IN INVERTEBRATES. THE PURIFICATION OF A HAEMAGGLUTININ TO RAT AND RABBIT ERYTHROCYTES FROM THE HAEMOLYMPH OF THE MURRAY MUSSEL ( Velesunio ambiguus ).
Author(s) -
Jenkin CR,
Rowley D
Publication year - 1970
Publication title -
australian journal of experimental biology and medical science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0004-945X
DOI - 10.1038/icb.1970.12
Subject(s) - hemolymph , centrifugation , biology , mussel , biochemistry , homogeneous , amino acid , chromatography , microbiology and biotechnology , chemistry , ecology , physics , thermodynamics
Summary A haemagglutinin present in the haemolymph of the Murray Mussel ( Velesunio ambiguus ) has been purified by density gradient centrifugation and elution from the specific red cell stroma. The purified haemagglutinin is one of several which behave as a homogeneous group of proteins. Amino acid analyses of these proteins indicate that they lack tyrosine and sulphur‐containing amino acids.