Über Hemmung des Kathepsins und Aktivierung des Papains durch α-Sulfhydrylcarbonsäuren.

Maschmann, Ernst; Helmert, Erica

doi:10.1515/bchm2.1933.222.5-6.207

Cited by 12 publications

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“…Although catalase is inhibited by simple iron(II) salts, neither bpy nor [Fe(bpy) 3 ] 2+ salts affect its activity [344]. Neither pepsin nor the cathepsins are inhibited by bpy [345]. Although the biological effects of [Fe(bpy) 3 ] 2+ were beginning to be documented, the stability of the complex led Eicholtz to classify it with the porphyrins and the hexacyanoferrates as a type of compound in which the iron is not biologically available [346].…”

Section: 1930–1939—golden Years and Then Back Into The Abyssmentioning

confidence: 99%

The Early Years of 2,2′-Bipyridine—A Ligand in Its Own Lifetime

2019

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The first fifty years of the chemistry of 2,2′-bipyridine are reviewed from its first discovery in 1888 to the outbreak of the second global conflict in 1939. The coordination chemistry and analytical applications are described and placed in the context of the increasingly sophisticated methods of characterization which became available to the chemist in this time period. Many of the “simple” complexes of 2,2′-bipyridine reported in the early literature have been subsequently shown to have more complex structures.

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Section: 1930–1939—golden Years and Then Back Into The Abyssmentioning

confidence: 99%

The Early Years of 2,2′-Bipyridine—A Ligand in Its Own Lifetime

2019

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“…There had been no report of synthesized plasmin in hibitors until 1950. As α-SH carboxylic acid and β-SH carboxylic acid were reported to have completely differ ent actions on cathepsin and papain, 1 the investigation was begun with SH compounds and derivatives, and certain relationships between the chemical structure and the antifibrinolytic activity were found; however, no po tent plasmin inhibitor was found in such compounds. Next, they investigated amino acids, and found that glu tamic acid and aspartic acid, both with negative charges, slightly elevated fibrinolytic activity; in contrast, lysine, with positive charges, inhibited fibrinolytic activity of plasmin.…”

Section: Plasmin-controlling Medicines: Eaca and T-amchamentioning

confidence: 99%

Enzyme-Controlling Medicines: Introduction

Okamoto¹,

Hijikata-Okunomiya²,

Wanaka³

et al. 1997

Semin Thromb Hemost

103

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A short history of the research work of S. Okamoto and co-workers, for the previous 50 years, is briefly described. In the 1950s, when the physiologic role of fibrinolysis had not been established, they began to seek for compounds that inhibit the action of plasmin. They examined approximately 200 lysine derivatives and discovered epsilon aminocaproic acid (EACA) and tranexamic acid (t-AMCHA). In the 1970s, we selected thrombin as the target enzyme to be controlled; structure-activity relationship studies, taking arginine as the skeleton structure, led to the discovery of the selective thrombin inhibitor No. 205 (4-ethyl-1-[N2-(5-dimethylamino-1-naphthalenesulfonyl)-L-arginyl]- 1-piperidine), and further attempts to minimize the toxicity finally led to No. 805 (argatroban, MD-805, (2R,4R)-4-methyl-1-(N2-[(3-methyl-1,2,3,4-tetrahydro-8-quinolinyl)-sulfo nyl]-L-arginyl)-2-piperidine carboxylic acid). Argatroban, without any cofactor, inhibits thrombin competitively. The high selectivity of the action of argatroban is promising for treating thrombosis in clinical practice. More recently, taking advantage of our knowledge obtained through previous studies, active center-directed plasmin inhibitors and a selective inhibitor of kallikrein have been found.

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Thiol Groups of Biological Importance

Barrón¹

1951

Advances in Enzymology - And Related Areas of Molecular Biology

117

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Über Hemmung des Kathepsins und Aktivierung des Papains durch α-Sulfhydrylcarbonsäuren.

Cited by 12 publications

References 0 publications

The Early Years of 2,2′-Bipyridine—A Ligand in Its Own Lifetime

The Early Years of 2,2′-Bipyridine—A Ligand in Its Own Lifetime

Enzyme-Controlling Medicines: Introduction

Thiol Groups of Biological Importance

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