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  1. No Access

    Article

    The juxtaglomerular apparatus in Bartter's syndrome and related tubulopathies

    A comparative immunocytochemical and electron microscopic study was performed on renal biopsies from two children with classical Bartter's syndrome (BS) and three children with a recently described variant, th...

    R. Taugner, R. Waldherr, H. W. Seyberth, E. G. Erdös, J. Menard… in Virchows Archiv A (1988)

  2. No Access

    Chapter and Conference Paper

    Hydrolysis of Peptide Bonds and Control of Blood Pressure

    Activation of proteases can affect the blood pressure in several ways. Activation of the renin, kallikrein, plasmin, and complement systems leads to the release of vasoactive peptide such as kinins, angiotensi...

    E. G. Erdös, T. A. Stewart in Biological Functions of Proteinases (1979)

  3. No Access

    Chapter

    Kininases

    Since publication of the previous edition of this Handbook in 1970, much new information has been gathered about kininases, the enzymes that inactivate kinins. This chapter provides a survey and update of rese...

    E. G. Erdös in Bradykinin, Kallidin and Kallikrein (1979)

  4. No Access

    Article

    Inhibition of the angiotensin I converting enzyme of the lung by a peptide fragment of bradykinin

    Nachweis, dass Arg-Pro-Pro, das N-terminale Tripeptid von Bradykinin, für die Hemmung der Konversion von Angiotensin I zu Angiotensin II in der Lunge verantwortlich ist.

    G. Oshima, E. G. Erdös in Experientia (1974)

  5. No Access

    Article

    Cleavage of active peptides by a lung enzyme

    Ein Enzym (Angiotensin I «converting enzyme» oder Kininase II; DH) wurde aus Schweinelungen isoliert und gereinigt. DH splatet Dipeptide vom Carboxyterminus der Peptidsubstrate mit Einschluss von Bradykinin, A...

    R. Igic, H. S. J. Yeh, K. Sorrells, E. G. Erdös in Experientia (1972)

  6. No Access

    Chapter

    Identity of Kininase II with an Angiotensin I Converting Enzyme

    Blood and tissues contain various enzymes that hydrolyze bradykinin. Among the ones we characterized were a prolidase (imidopeptidase), a carboxypeptidase-type enzyme (carboxypeptidase N; kininase I) and a dip...

    R. Igic, K. Sorrells, T. Nakajima, E. G. Erdös in Vasopeptides (1972)

  7. No Access

    Article

    Properties of granules that contain kallikrein and renin

    Subzelluläre Partikel, die Renin und Kallikrein enthalten, wurden durch Differentialzentrifugation aus homogenisierter Submaxillardrüse der männlichen weissen Maus angereichert. Durch Zonenzentrifugation wurde...

    F. Geipert, E. G. Erdös in Experientia (1971)

  8. No Access

    Chapter

    Enzymes that Inactivate Vasoactive Peptides

    This chapter deals with the enzymatic inactivation of two types of vasoactive peptides, plasma kinins and angiotensin II. The metabolic fate of other hormonal or exogenous peptides is not discussed here.

    E. G. Erdös in Concepts in Biochemical Pharmacology (1971)

  9. No Access

    Article

    Active Water-insoluble Derivative of Renin

    ALTHOUGH the action of renin on the blood pressure has been explored by many investigators, some of its basic enzymatic properties are yet to be established1. While studying plasma kinins, we found it to be of ad...

    T. SEKI, T. A. JENSSEN, Y. LEVIN, E. G. ERDÖS in Nature (1970)

  10. No Access

    Chapter

    Application of Water-Insoluble Complexes of Kininogenases, Inhibitors and Kininases to Kinin Research

    Although a variety of methods have been available for coupling proteins with water-insoluble carriers, the impetus to our experiments was given by a publication of Levin et al. (1). They coupled trypsin to the co...

    T. Seki, H. Y. T. Yang, Y. Levin, T. A. Jenssen… in Bradykinin and Related Kinins (1970)

  11. No Access

    Chapter

    Kininases

    Kininases are enzymes that inactivate kinins This chapter will survey them together with other enzymes that can convert some of the longer analogs of bradykinin to the nonapeptide.

    E. G. Erdös, H. Y. T. Yang in Bradykinin, Kallidin and Kallikrein (1970)

  12. No Access

    Article

    New Enzymatic Route for the Inactivation of Angiotensin

    Experiments show that swine kidney and human urine contain a new angiotensinase that breaks the prolylphenylalanine bond In various peptides. The product of this enzymatic hydrolysis—the N-terminal heptapeptid...

    H. Y. T. YANG, E. G. ERDÖS, T. S. CHIANG in Nature (1968)

  13. No Access

    Article

    Second Kininase in Human Blood Plasma

    COHN fraction IV-1 of human plasma contains an enzyme, carboxypeptidase N, which inactivates bradykinin and kallidin1,2 and also cleaves smaller substrates such as hippuryl-L-lysine (HLL)3. The kininase also has ...

    H. Y. T. YANG, E. G. ERDÖS in Nature (1967)

  14. No Access

    Article

    Über eine neue blutdrucksenkende, darm-und uteruserregende Substanz im menschlichen Urin

    Es wird die Anreicherung einer neuen im menschlichen Harn vorkommenden blutdrucksenkenden, darm- und uteruserregenden Substanz beschrieben. Es handelt sich sehr wahrscheinlich um ein Polypeptide. Die neue Subs...

    E. Werle, E. G. Erdös in Naunyn-Schmiedebergs Archiv für experiment… (1954)