Search

Summary Precipitating antisera against human serum albumin, α2-macro-globulin, siderophilin and gammaglobulin were tested against the sera of different mammals (rhesus monkey, horse, cow, cat, dog, sheep, pig, guinea pig, mouse, hedgehog), using Ouchterlony's agar diffusion method. Based on the heterologous precipitin reactions it is possible to conclude that human serum albumin must contain at least 11, α2-macroglobulin at least 8, siderophilin at least 4 and gamma-globulin at least 6 different antigenic determinants. The proteins of the rhesus monkey contain at least one such determinant group less than the corresponding human proteins. The corresponding proteins of the other mammals tested contain determinant groups in common with the human serum proteins in varying number and distribution. These results suggest that immune sera against protein antigens consist of numerous different antibodies, each one directed against a specific determinant group of the antigen. Resume Des immunserums precipitants anti-albumine serique, anti-α2-macroglobuline, anti-siderophiline et anti-γ-globuline humaine ont ete testes par la methode de precipitation dans l'agar selon Oucherlony avec des serums de differents mammiferes (singe Rhesus, cheval, bovide, chat, chien, mouton, porc, cobaye, souris et herisson). Ces precipitations heterologues ont montre que chez l'homme l'albumine serique contient au moins 11, l'α2-macroglobuline au moins 8, la siderophiline au moins 4 et la γ-globuline au minimum 6 determinants antigeniques. Chez le singe Rhesus ces memes 4 proteines seriques contiennent au moins un determinant antigenique commun de moins que chez l'homme. Chez les autres mammiferes le nombre de la repartition des determinants communs aux proteines de l'homme est variable. Ces experiences montrent qu'un immunserum antiprotidique contient de nombreux anticorps differents, reagissant chacun specifiquement avec le determinant antigenique donne. Zusammenfassung Prazipitierende Immunseren gegen menschliches Serumalbumin, α2-Makroglobulin, Siderophilin und γ-Globulin wurden im Agar-diffusionstest nach Ouchterlony gegen verschiedene Saugetierseren (Rhesusaffe, Pferd, Rind, Katze, Hund, Schaf, Schwein, Meerschweinchen, Maus, Igel) angesetzt. Anhand der heterologen Prazipitations-reaktionen gelang es zu zeigen, das das menschliche Serumalbumin mindestens 11, das α2-Makroglobulin mindestens 8, das Siderophilin mindestens 4 und das γ-Globulin mindestens 6 differente Antigen-determinanten aufweisen. Die entsprechenden Proteine des Rhesus-affenserums enthalten mindestens eine gemeinsame Determinante weniger als die menschlichen Proteine. In den entsprechenden Proteinen der ubrigen Saugetiere sind die restlichen im menschlichen Serumprotein vorkommenden Determinanten in wechselnder Zahl und Verteilung vorhanden. Auf Grund dieser Untersuchungen ist anzunehmen, das Immunseren gegen Proteine zahlreiche Antikorper enthalten, die mit den betreffenden Determinanten des Antigens spezifisch reagieren.

Changes in the N-terminal amino acids of bovine and human fibrinogen and fibrin resulting from the action of plasmin (EC 3.4.4..14) on these protinens have been studied. Only the N-terminal amino acids of those protein fractions whose phenylthiocarbamyl derivatives are insoluble in acetone-water have been measured. Plasminolysis of the bovine and human proteins leads to similarities and differences in the relative rates at which N-termnial residues appear. Possible causes for these differences are discussed. The observations explain in part the presence of extraneous N-terminal residues frequently found in fibrinogen, particularly if isolated from aged Fraction I preparations, and provide preliminary information which may be useful as a guide during the separation of fragments formed during the proteolysis of fibrinogen.

MANY human proteins exist in more than one genetically determined variety1, but no polymorphism has been reported in human milk proteins, although some components have been sufficiently characterized from the biochemical standpoint2,3 and extensive polymorphism has been detected in cow's milk. We therefore decided to investigate the possible occurrence of polymorphic variants of human casein, since electrophoresis has now given a clear picture of bovine casein genetics, which can be used as a model for study of the situation in man4,5. Such variants would obviously be more easily used as genetic markers at the population than at the family level. Moreover, data reported by Grosclaude et al.6 suggest the existence of a supergene controlling bovine αs1, β and k-caseins. For this reason, the possibility of a similar genetic control of human polymorphism (if any) was also tested.

From time to time attempts have been made to determine the source of the protein present in albuminous urine. Chemical methods are, in most forms of albuminuria, entirely incapable of distinguishing between blood proteins, kidney proteins and urinary proteins. The most definite exception to this statement is furnished by the peculiar protein of "myelopathic albumosuria," which is distinctly different from any protein found in normal blood or tissues. With the advent of the precipitin reaction came the possibility of distinguishing sharply between proteins from different species of animals, which made it feasible to investigate the urinary proteins in relation to their original source, i. e., to determine whether they come unchanged from the food proteins, or have the character of human proteins. Several studies of this kind have been reported, but not with constant results. So discordant and widely scattered is the literature on this topic that it

The detection of antibodies against human erythrocytes is important in the diagnosis of hemolytic anemia, erythroblastosis fetalis, and transfusion reactions and is essential for crossmatching blood before transfusion. Such antibodies belong to the immunoglobulin group of proteins. The immunoglobulin-S are IgG, the most common; IgM; and IgA. Tests for blood group antibodies must detect antibody protein of all three immunoglobulin types. While no one test will do this for every antibody, the Coombs' (antiglobulin) test is the best because it reacts with most antibodies in each class of immunoglobulin. The test is done with antiglobulin serum, an anti-antibody type of reagent produced in laboratory animals. Rabbits injected with human serum produce antibodies to human proteins. Serum from such immunized animals, when properly prepared, can be used as an anti-antibody to detect human immunoglobulins, particularly those that have reacted with erythrocytes. In the Coombs' test, erythrocytes coated with antibody are agglutinated

The solution of the very important and difficult problems presented by progressive deafness due to otosclerosis—its cause, prevention, and cure—is to be found in the biological implications and applications of the newly acquired and as yet incompletely correlated data in the field of ultrasonics. As there are light waves which are beyond the physiological range of human visual perception, there are sound waves that are imperceptible to the human ear—the ultrasonics. The most silent centrifuge has an ultrasonic specter extending to 100 000 cy/sec. The telephone bell produces frequencies to 50 000 cy/sec, powerful, but silent, imperceptible to us. The traffic of everyday life, in the train, bus, car, next to the audible noise, hides a tremendous amount of silent sound which is frightfully dangerous to our hearing organ. A significant fact of modern research is that the intensities of ultrasonics are of not primary importance in influencing the chemical changes in human proteins. Sonics and ultrasonics are e...