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J L FAHEY

Publications and source records attributed to J L FAHEY.

At least 19 recordsLinked to original sources
PubMed1965

THE IMMUNOGLOBULINS OF MICE. V. THE METABOLIC (CATABOLIC) PROPERTIES OF FIVE IMMUNOGLOBULIN CLASSES.

The metabolic properties of immunoglobulin were investigated by comparing five classes of mouse immunoglobulin. Three forms of 7S immunoglobulin had different rates of catabolism. The fractional rates of catabolism were found to be about 13 per cent per day for 7S gamma(2a)-globulin; 25 per cent for 7S gamma(2b)-globulin; and 17 per cent for 7S gamma(1)-globulin. Catabolism of the three classes of 7S gamma-globulin (gamma(2a), gamma(2b), and gamma(1)) were prolonged at low serum 7S gamma-globulin levels and accelerated at high serum 7S gamma-globulin levels. Each of the 7S gamma-globulin components was influenced by the serum level of the other mouse 7S gamma-globulin components and by exogenously administered human 7S gamma-globulin. They were not appreciably altered, however, by the serum level of IgA (gamma(1)A-, beta(2)A-globulin). The progressively changing (longer) half-times observed in turnover studies of normal IgG (7S gamma-globulin) may be caused by catabolic heterogeneity of normal 7S immunoglobulins which are immunochemically and catabolically related to gamma(2a)-, gamma(2b)-, and 7S gamma(1)-myeloma proteins. These studies indicate that the 7S gamma(2a)-, 7S gamma(2b)-, and 7S gamma(1)-globulins share a common catabolic control mechanism. This mechanism is influenced by the serum level of each of these components, but is independent of the serum level of IgA (gamma(1)A-globulin) and probably is independent of IgM (gamma(1)M-globulin). Catabolism of IgA (gamma(1)A-, beta(2)A-globulin) and IgM (gamma(1)M-globulin) was much more rapid than the catabolism of the 7S gamma-globulins. The halftimes of the IgA and IgM were approximately 1.2 and 0.5 days respectively. The fractional rate of catabolism of IgA and IgM seemed to be independent of their serum concentration. The rate of catabolism, as well as the rate of synthesis, was shown to play a major role in determining the serum level of each class of immunoglobulin.

Animals↗
PubMed1965

A NEW CLASS OF HUMAN IMMUNOGLOBULINS. I. A UNIQUE MYELOMA PROTEIN.

The unique myeloma protein from S. J., a patient with multiple myeloma, was isolated and characterized. It resembled other myeloma proteins in many respects. The S. J. myeloma protein migrated in a distinct peak in the slow beta-globulin region on zone electrophoresis, appeared as a single band on starch gel electrophoresis, and sedimented at 7.04S in the ultracentrifuge. Papain and cysteine treatment produced Fc (fast) and Fab (slow) fragments. Reduction and alkylation of the myeloma protein produced heavy and light chains in a ratio of approximately 3:1. The S. J. myeloma protein had type L (type II) light chains. These were antigenically similar to the Bence Jones protein also found in this patient. The S. J. myeloma protein was unique in the properties of its heavy chains. The myeloma protein (and its heavy chains and Fc pieces) did not contain antigenic determinants specific for IgG, IgA, or IgM. The myeloma protein (and its heavy chains), however, did contain antigenic determinants which are characteristic of a new class of immunoglobulin. The S. J. myeloma protein was unusual also in its effect on the metabolism of normal IgG and in the electrophoretic mobility of the Fc fragment produced by papain digestion. No evidence was obtained to indicate that the entire heavy polypeptide of the S. J. protein was a grossly abnormal product of malignant cell metabolism. The unique properties of the S. J. myeloma protein (and its heavy chains) are believed to represent, in large measure, properties to be found in a small part of the normal immunoglobulin population.

Animals↗
PubMed1965

A NEW CLASS OF HUMAN IMMUNOGLOBULINS. II. NORMAL SERUM IGD.

A new class of immunoglobulin, IgD, was identified in normal human serum by immunochemical technics. Antiserums prepared against the unique S.J. myeloma protein facilitated recognition of the related normal protein. IgD was shown to possess type K (I) and type L (II) light chain determinants, similar to those present in other classes of immunoglobulins. IgD does not possess determinants which are specific to IgG, IgA, or IgM. The IgD proteins possess their own specific antigenic determinants. IgD migrates in the fast gamma-region on immunoelectrophoresis. The properties on sephadex gel filtration and DEAE cellulose chromatography are described. IgD was found to have a median level of 0.03 mg/ml in 100 normal serums. The range of concentrations found in individual normal serums is much wider, however, than that of other classes of immunoglobulins. IgD, on the average, accounts for less than 1 per cent of the normal serum immunoglobulins.

Animals↗
PubMed1964

SUBCLASSES OF HUMAN GAMMA-2-GLOBULIN BASED ON DIFFERENCES IN THE HEAVY POLYPEPTIDE CHAINS.

Three subclasses of human gamma(2)-globulin (IgG) molecules were detected in normal human serum with antiserums prepared in monkeys. These subclasses, designated gamma(2a)-, gamma(2b)-, and gamma(2c)-globulins, have antibody activity. The distinguishing antigenic characteristics of each subclass were associated with the heavy polypeptide chains and the F (fast) fragments resulting from treatment of gamma(2)-globulins with papain.

Antigens↗
PubMed1964

THE IMMUNOGLOBULINS OF MICE. I. FOUR MAJOR CLASSES OF IMMUNOGLOBULINS: 7S GAMMA-2-, 7S GAMMA-1-, GAMMA-1A (BETA-2A)-, AND 18S GAMMA-1M-GLOBULINS.

Two classes of 7S gamma-globulins are identified in normal mouse serum and are designated 7S gamma(2)-globulins and 7S gamma(1)-globulins. These two immunoglobulin classes are similar in size. They differ in range of electrophoretic mobility, in specific antigenic determinants, and in genetically determined isoantigens. Four classes of immunoglobulins in mouse serum, i.e. 7S gamma(2)-, 7S gamma(1)-, gamma(1A) (beta(2A)), and gamma(M)-globulins, were shown to have antibody activity. Each class was characterized and shown to have distinctive immunochemical and physicochemical properties. The genetically determined isoantigens, Iga-1 and Iga-2, were shown to be present only on 7S gamma(2)-globulin molecules.

Animals↗
PubMed1964

THE IMMUNOGLOBULINS OF MICE. II. TWO SUBCLASSES OF MOUSE 7S GAMMA-2-GLOBULINS: GAMMA-2A- AND GAMMA-2B-GLOBULINS.

Two subclasses of mouse 7S gamma(2)-globulins are identified, and are designated gamma(2a)- and gamma(2b)-globulins. They are distinguished from 7S gamma(1)-globulins, gamma(1A) (beta(2A))-globulins, and gamma(1M)-globulins of mouse serum. Antibody activity was detected among the gamma(2a)-globulins and gamma(2b)-globulins of hyperimmune mouse serum. gamma(2a)- and gamma(2b)-myeloma proteins were identified. The genetically determined isoantigen, Iga-1, was present on gamma(2a)-myeloma proteins, but not on gamma(2b)-myeloma proteins. These findings indicate a complexity among the 7S gamma(2)-globulins which must be taken into account in structural, functional, and genetic studies of immunoglobulins.

Animals↗
PubMed1964

MOLECULAR AND SUBMOLECULAR LOCALIZATION OF TWO ISOANTIGENS OF MOUSE IMMUNOGLOBULINS.

Three related classes of immunoglobulins ( 7S gamma(-), beta(2)A(-), and gamma(1)M(-) globulin) in normal C3H and C3H and C57BL/6 mouse serums were isolated and examined for the isoantigens Iga-1 and Iga-2. The results indicate that the genetic locus determining the Iga-1 and Iga-2 antigens affects only a portion of the normal mouse immunoglobulin population (that is, 7S gamma-globulin) and only the gamma-specific part ("F" piece) of the 7S gamma-globulin molecule.

Animals↗
PubMed1964

ANTIBODY ACTIVITY IN SIX CLASSES OF HUMAN IMMUNOGLOBULINS.

Antibody activity to thyroglobulin was identified in six classes of immunoglobulins in man, that is, in type I and type II, 6.6S gamma-globulins; in type I and type II, beta(2A)-globulins; and in type I and type II, gamma(1)-macroglobulins. These observations indicate that antibody-activity sites are separate from the part of the H chains of immunoglobulin molecules responsible for specific properties of 6.6S gamma-globulin, beta(2A)-globulin, or gamma(1M)-globulin, and, also, are separate from the part of L chains responsible for type I or type II characteristics of immunoglobulin molecules.

Antibodies↗