Abstract
Three anticoagulant proteins were isolated from the venom of Naja nigricollis (spitting cobra). The peaks of anticoagulant activity co-chromatographed with phospholipase A2 activities. The three proteins were homogeneous by the criteria of electrophoresis in two acidic polyacrylamide gel systems. Electrophoresis in sodium dodecyl sulfate also yielded single protein bands with molecular weights of about 15,000. The amino acid compositions of the three anticoagulant proteins are reported. All three proteins have only one amino acid replacement in the first 25 to 30 amino acids of their NH2-terminal sequences, compared to the sequence of the basic phospholipase from N. nigricollis venom. Removal of Ca2+ from the crude venom caused loss of both anticoagulant and phospholipase activities, and restoration of Ca2+ caused partial recovery of both activities. Both activities were lost in parallel when the venom was heated between pH 6.0 and 8.5. The association of the anticoagulant effect with phospholipase activity contradicts the previous conclusion that phospholipase is not responsible for the anticoagulant action of cobra venom. The previous results might be explained by independence of the anticoagulant and phospholipase effects within the same protein molecule, or by different activity levels of monomer and dimer forms of the enzyme.
Highlights
From the Departments of Biochemistry, Biophysics, and Medicine, Medical College of Virginia, Virginia Commonwealth University, Richmond, Virginia 23298
A similar independence venom ofNaja nigricollis.The peaks of of the anticoagulant and phospholipase effects might anticoagulant activity co-chromatographed with phos- account for the earlier results with cobra venom [1]
Three of the four anticoagulant peaks from carboxymethyl Bio-Gel chromatography (CM-I, CM-11, and CM-IV) were homogeneous by the criteria of electrophoresis in two acidic polyacrylamide gel systems, SDS-polyacrylamide gel electrophoresis and amino acid sequencing.The pool labeled CM-111 was obviously heterogeneous in the electrophoretic analysis, but it contained a protein which migrated in the same position as CM-IV,suggesting that CM-IV might be eluted intwo forms
Summary
From the Departments of Biochemistry, Biophysics, and Medicine, Medical College of Virginia, Virginia Commonwealth University, Richmond, Virginia 23298. From theHematology Diviswn, Center for DiseaseControl, Public HealthService, United States Department of Health, Education, and Welfare, Atlanta, Georgia 303333. Three anticoagulant proteins wereisolated from the the activities within the same protein. A similar independence venom ofNaja nigricollis (spitting cobra).The peaks of of the anticoagulant and phospholipase effects might anticoagulant activity co-chromatographed with phos- account for the earlier results with cobra venom [1]. Electrophoresisin sodium proached the question of the involvement of phospholipase in dodecyl sulfate yielded single protein bands with the anticoagulant effect by resolution of the proteins of the molecular weights ofabout 15,000. Theaminoacid crude venom and study of the anticoagulant and phospholicompositions of the three anticoagulant proteins are pase Azactivities of the highly purified proteins. All three proteins have only one amino acid replacement in the first 25 to 30 amino acids of their
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