The carbohydrate side chains of the major plasma serpins of horse and wallaby: analyses of enzymatic and chemically treated (including 'Smith degradation') protein blots by lectin binding.
The carbohydrate side chains of the major plasma serpins of the horse and wallaby have been characterized by lectin analyses of protein blots from two-dimensional gels using the major human plasma serpin, alpha 1-protease inhibitor, as a control. Eight lectins were used in the characterization in conjunction with enzymatic deglycosylation of complex and high mannose side chains, chemical desialylation and defucosylation, and one round of 'Smith degradation', all being performed on the nitrocellulose blots. Assuming a standard complex side chain structure, the results of the 21 lectin/treatment combinations were interpreted as indicating that the equine proteins consist of partially sialylated biantennary side chains except for the most acidic proteins which have triantennary side chains. The wallaby proteins have bi- and triantennary side chains with a bisecting N-acetylglucosamine and fucose residue present.
Patterson
S D
SD
Department of Physiology and Pharmacology, University of Queensland, St. Lucia, Australia.
Bell
K
K
D000818:Animals; D015153:Blotting, Western; D002240:Carbohydrate Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases; D006736:Horses / Q000097:blood*; D006868:Hydrolysis; D037102:Lectins; D007614:Macropodidae / Q000097:blood*; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D008394:Marsupialia / Q000097:blood*; D008969:Molecular Sequence Data; D015843:Serpins / Q000097:blood*
D037102:Lectins; D015843:Serpins; D006026:Glycoside Hydrolases; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase