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K NISHIOKA

Publications and source records attributed to K NISHIOKA.

At least 19 recordsLinked to original sources
PubMed1963

COMPONENTS OF GUINEA PIG COMPLEMENT. I. SEPARATION OF A SERUM FRACTION ESSENTIAL FOR IMMUNE HEMOLYSIS AND IMMUNE ADHERENCE.

Employing sheep erythrocytes sensitized by antibody and the first and fourth components of complement (EAC'1,4), in such a manner as to prevent the development of immune adherence (I-A) reactivity during preparation, four separate substances required for the conversion of EAC'1,4,2 to the final damaged state (E*) were identified in whole guinea pig serum by cellulose chromatography, and tentatively termed C'3c, C'3b, C'3a, and C'3d. I-A reactivity was induced in EAC'1,4,2 after interaction with only one of these four substances, C'3c. A detailed comparison of the effects of heat, hydrazine, low pH, freezing, absorption by immune complexes, and elution from cellulose columns indicated that this same substance which was capable of imparting I-A reactivity to EAC'1,4,2 was also essential for immune hemolysis. Other experiments showed that I-A-reactive cells prepared either by treating EA with different concentrations of whole C' at 0 degrees C, or by treating EAC'1,4,2 with C'3c, underwent lysis by C'2 + C'3b + a + d in proportion to the amount of whole C' or of C'3c used to make the cells reactive in I-A. These data provide strong evidence that a single factor, C'3c, is required both for the conversion of EAC'1,4,2 to an I-A-reactive complex (EAC'1,4,2,3c) and for the lysis of EAC'1,4,2 by C'3b + a + d. C'3c is the only one of the components studied which can induce I-A reactivity, and is the first to react with EAC'1,4,2. Formation of EAC'1,4,2,3c proceeds even at 0 degrees C, but is much more rapid at elevated temperatures, showing a maximum in from 5 to 15 minutes at 37 degrees or 30 degrees C respectively. Prolonged incubation at these temperatures results in a decline in hemolytic reactivity without a noticeable effect on I-A. This loss was resolved into three phenomena: (a) a rapid loss of ability of SAC'1,4,2,3c to react with C'3b, presumably as a result of decay of the C'2 moiety in the complex, which is readily reversed by addition of fresh C'2; (b) a slow, irreversible spontaneous inactivation of SAC'1,4,2,3c; (c) a moderately rapid, irreversible inactivation of SAC'1,4,2,3c by some factor present in C'3c preparations.

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PubMed1963

COMPONENTS OF GUINEA PIG COMPLEMENT. II. SEPARATION OF SERUM FRACTIONS ESSENTIAL FOR IMMUNE HEMOLYSIS.

The elution characteristics from DEAE cellulose are presented for four components of guinea pig serum, which are capable of interacting sequentially with sheep erythrocytes sensitized with antibody and the first, fourth, and second components of complement (EAC'1,4,2) to cause immune hemolysis, and information is given regarding some of the properties of these components, termed C'3c, C'3b, C'3a, and C'3d. All can react in the presence of ethylene-diaminetetraacetate, and are non-dialyzable. C'3c is quite stable at 56 degrees C, but is rapidly inactivated at low pH or by contact with hydrazine or ammonium hydroxide. C'3b is moderately heat-stable, quite susceptible to low pH, and less readily destroyed by hydrazine. C'3a is very heat-labile, but relatively stable at low pH, while C'3d is heat-labile, sensitive to low pH, and insensitive to bydrazine. EAC'1,4,2 reacts with C'3c to form EAC'1,4,2,3c, which reacts then with C'3b to give the intermediate, EAC'1,4,2,3cb. The following reaction with C'3a yields EAC'1,4,2,3cba, which reacts finally with C'3d to give EAC'1,4, 2,3cbad (E*). The first and last reactions proceed moderately well at 0 degrees C, but more rapidly at 30-37 degrees C. The reaction with C'3b is almost completely inhibited at 0 degrees C, while that involving C'3a proceeds almost as rapidly at 0 degrees C as at higher temperatures. EAC'1,4,2,3cba cells have an increased fragility as compared with the other intermediate forms. Depletion studies with purified fractions and appropriate intermediate complexes showed a high degree of depletion of C'3c, somewhat less of C'3b, and little or no depletion of C'3a from the fluid phase. Examination of a beta(1C) globulin prepared from fresh human serum revealed high C'3c and C'3b activity, and very little C'3a or C'3d.

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