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Cited by 41 publications
References 7 publications
GL OBUL I NS LOBULINS which bind in vitro to cross striations of skeletal muscle, as demonstrated by immunofluorescent techniques, were first reported in the serums of patients with myasthenia gravis by Strauss and associates.1 These globulins have been reported to bind to striations of skeletal muscle from experimental animals, normal humans, and myasthenic patients, including patients from whom serum was obtained.2-5 The presence of the striation binding globulin has been reported in the serum of 18% to 68% of patients with myasthenia gravis,1,4-10 and the binding activity of the globulin tends to be higher in myasthenic patients with more severe conditions4-7,9-11 and with thymoma.11-13 Serum globulin bound to cross striations was found in excised muscle in two of five myasthenic patients examined by Gordon and associates14 and in two of four patients examined by Beutner and associates.15 The serums of all of these patients contained a globulin which was capable of binding in vit¬ ro with skeletal muscle striations. Opinion has differed whether this binding occurred in vivo15 or only after biopsy of the muscle or the death of the patient.14 In the present study, the muscles of ten myasthénie patients have been examined for the presence of striation-binding globulin, and the binding of globulin in vivo to rat skeletal muscle has been investigated follow¬ ing injection of serum from patients with myasthenia gravis. Similar observations in vivo have also been made on the antiserums formed against rat skeletal muscle constitu¬ ents. Materials and MethodsThe gastrocnemius or deltoid muscle was ob¬ tained by biopsy from eight patients with myasthenia gravis. The intercostal and rectus abdominus muscles were obtained at autopsy within five hours of death from two patients with myasthenia gravis (No. 297 and 575) and from 20 patients who had diseases unrelated to the neuromuscular system. The muscle, imme¬ diately frozen in dry ice-isopentane, was sec¬ tioned 4µ thick in a cryostat at -23 C, dried on a cover slip by a stream of air, and fixed in ace¬ tone for ten minutes at 4 C. Serum globulins in the section were then localized by staining for 60 minutes at room temperature with fluorescein-labeled antihuman serum globulins, in¬ cluding antihuman serum globulin, antihuman serum IgG (yG, 2, or 7S globulin), antihu¬ man serum IgA (yA, , or /32A), and antihuman serum IgM (yM, YlM, /32M, or 19S globulin).ie All antiglobulins were of caprine origin. The globulin fraction of these antiserums or goat serum did not bind with human muscle, rat muscle, rat serum, or rabbit serum.Human serums were obtained from 13 pa¬ tients with myasthenia gravis, 20 patients with diseases unrelated to the neuromuscular sys¬ tem, and 20 normal subjects. Antiserums against constituents of rat skeletal muscle were prepared by intramuscular injection in rabbits of muscle homogenate, saline extract of muscle, muscle ribonucleoprotein, or actomyosin, re¬ spectively. These substances, containing 50 mg of protein, were used as antigens and injected t...
GL OBUL I NS LOBULINS which bind in vitro to cross striations of skeletal muscle, as demonstrated by immunofluorescent techniques, were first reported in the serums of patients with myasthenia gravis by Strauss and associates.1 These globulins have been reported to bind to striations of skeletal muscle from experimental animals, normal humans, and myasthenic patients, including patients from whom serum was obtained.2-5 The presence of the striation binding globulin has been reported in the serum of 18% to 68% of patients with myasthenia gravis,1,4-10 and the binding activity of the globulin tends to be higher in myasthenic patients with more severe conditions4-7,9-11 and with thymoma.11-13 Serum globulin bound to cross striations was found in excised muscle in two of five myasthenic patients examined by Gordon and associates14 and in two of four patients examined by Beutner and associates.15 The serums of all of these patients contained a globulin which was capable of binding in vit¬ ro with skeletal muscle striations. Opinion has differed whether this binding occurred in vivo15 or only after biopsy of the muscle or the death of the patient.14 In the present study, the muscles of ten myasthénie patients have been examined for the presence of striation-binding globulin, and the binding of globulin in vivo to rat skeletal muscle has been investigated follow¬ ing injection of serum from patients with myasthenia gravis. Similar observations in vivo have also been made on the antiserums formed against rat skeletal muscle constitu¬ ents. Materials and MethodsThe gastrocnemius or deltoid muscle was ob¬ tained by biopsy from eight patients with myasthenia gravis. The intercostal and rectus abdominus muscles were obtained at autopsy within five hours of death from two patients with myasthenia gravis (No. 297 and 575) and from 20 patients who had diseases unrelated to the neuromuscular system. The muscle, imme¬ diately frozen in dry ice-isopentane, was sec¬ tioned 4µ thick in a cryostat at -23 C, dried on a cover slip by a stream of air, and fixed in ace¬ tone for ten minutes at 4 C. Serum globulins in the section were then localized by staining for 60 minutes at room temperature with fluorescein-labeled antihuman serum globulins, in¬ cluding antihuman serum globulin, antihuman serum IgG (yG, 2, or 7S globulin), antihu¬ man serum IgA (yA, , or /32A), and antihuman serum IgM (yM, YlM, /32M, or 19S globulin).ie All antiglobulins were of caprine origin. The globulin fraction of these antiserums or goat serum did not bind with human muscle, rat muscle, rat serum, or rabbit serum.Human serums were obtained from 13 pa¬ tients with myasthenia gravis, 20 patients with diseases unrelated to the neuromuscular sys¬ tem, and 20 normal subjects. Antiserums against constituents of rat skeletal muscle were prepared by intramuscular injection in rabbits of muscle homogenate, saline extract of muscle, muscle ribonucleoprotein, or actomyosin, re¬ spectively. These substances, containing 50 mg of protein, were used as antigens and injected t...
While introducing the method of fluorescent antibodies two samples of fluorescein isocyanate prepared independently in two laboratories were tried in 1957. The results obtained were unsatisfactory, the remaining fluorescence of the conjugates was weak. Therefore we searched for some other fluorescent stain that would be easier to synthetize and more suitable for routine work. The first tests with l-dimethylaminonaphthalene-5-sulpho-[49]
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