Das optische Auswählen der Leberesterase im System der „Ausgleichungsaktivatoren“. [IX. Mitteilung „Über asymmetrische Esterhydrolyse durch Enzyme.“]

Bamann, Eugen; Laeverenz, Paul

doi:10.1515/bchm2.1934.223.5-6.185

Hoppe-Seyler´s Zeitschrift für physiologische Chemie

1934

DOI: 10.1515/bchm2.1934.223.5-6.185

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Das optische Auswählen der Leberesterase im System der „Ausgleichungsaktivatoren“. [IX. Mitteilung „Über asymmetrische Esterhydrolyse durch Enzyme.“]

Eugen Bamann¹,

Paul Laeverenz²

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1935

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Cited by 9 publications

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“…The concept has been advanced that many enzymes are present in cells in at least two forms. The term "lyoenzyme" has been ascribed to the extractable component and "desmoenzyme" to the insoluble fraction which remained fixed to the cellular structural constituents (1)(2)(3). Lison (4) deserves credit for re-emphasizing the role of these two enzyme components in histochemical analysis.…”

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“…Such a study is particularly relevant at present to the proper evaluation of histochemical methods for enzymes. Questions which frequently arise are (1) how much of the enzyme is present in the lyo form, (2) what are the differences between various enzymes in this respect, and (3)what are some of the factors and conditions used in histochemistry which influence the diffusion of the lyo form? Experiments designed to answer these questions form the basis of this report.…”

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Quantitative Estimation of Lyo- And Desmoenzymes in Tissue Sections With and Without Fixation

Nachlas

Prinn

Seligman

1956

The Journal of Cell Biology

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The concept has been advanced that many enzymes are present in cells in at least two forms. The term "lyoenzyme" has been ascribed to the extractable component and "desmoenzyme" to the insoluble fraction which remained fixed to the cellular structural constituents (1-3). Lison (4) deserves credit for re-emphasizing the role of these two enzyme components in histochemical analysis. Investigators who have been developing or :employing histochemical techniques have been aware of the significant amount of enzyme which diffuses into the incubation medium. The appearance of the split product in the buffered substrate solution as well as in the tissue section has been a disturbing feature of many methods. Efforts to reduce this phenomenon have been partly successful by either exposing the tissues to fixatives before incubation, or by adding high concentrations of salts to the incubating solution. These attempts have met with varying degrees of success, depending to a large extent upon the enzyme being investigated, the degree of inhibition by these agents, and the solubility characteristics of the enzyme. Although a marked decrease in the amount of enzyme diffusing into the incubation solution may be attained under certain conditions, the extent of the movement of the enzyme within the cell and the exact amount of diffusion out of the tissue section is still undetermined.In recent years, Several quantitative methods have been employed in enzyme histochemistry, but these were not specifically designed to measure the lyo and desmo components of enzymes.

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confidence: 99%

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Quantitative Estimation of Lyo- And Desmoenzymes in Tissue Sections With and Without Fixation

Nachlas

Prinn

Seligman

1956

The Journal of Cell Biology

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“…The lauric acid liberated is titrated with phenol red. The author (21) has some doubts about the crystalline enzyme of Bamann & Laeverenz (22). New methods for extraction and pre cipitation are described.…”

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Nonoxidative Nonproteolytic Enzymes

Myrbäck¹

1949

Annu. Rev. Biochem.

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It has been, more or less, a tacit assumption that enzymes constitute only a small part of the protein of the living cell.Virtanen has pointed out that from our present knowledge of the quantities of enzymes it seems justifiable to conclude that in microorganisms practically all protein is enzyme protein. There fore, the formation of an adaptive enzyme should correspond to a decrease in some other enzyme or enzymes, presumably of a related type. Lowering of the protein content of the cell by starvation should decrease primarily the amounts of adaptable (dispensable) enzymes, whereas the indispensable (constitutive) enzymes should maintain their activity. Virtanen & De Ley (1) have determined saccharase in E. coli which is, in this case, an adaptive enzyme, and catalase, a typically constitutive enzyme. By nitrogen starvation the protein content of the cells could be materially decreased. The saccharase content fell rapidly but catalase activity was only slightly affected. Investigations by Bucher & Kaspers (2) on the photochemical splitting of carbon monoxide hemoglobin may throw light on the action of the protein carrier on the prosthetic groups of enzymes. Not only radiation absorbed by the hemin splits off carbon monoxide, but also radiation absorbed by the protein. In the photo inactivation of urease the effect is the same, if the quanta are absorbed by a few tyrosine or tryptophane residues or by all amino acids. It is suggested that transmission of absorbed activation energy may be one of the causes of the chemical activation of prosthetic groups by the carriers. Attention is called to a paper by Veldstra (3) on the interaction of "ergones" and substrates. Rothen's experiments on "enzyme action at a distance" were mentioned in Vol. XVII of this Review. New experiments (4) have been published which are thought to exclude the possibility of diffusion of the enzyme through the protecting layers. Mettler, however, points out (5) that the antigen films are not of constant 1 This review covers approximately the period from December, 1947 to De cember, 1948. 59 Annu. Rev. Biochem. 1949.18:59-86. Downloaded from www.annualreviews.org Access provided by Technische Universiteit Eindhoven on 02/02/15. For personal use only. Quick links to online content Further ANNUAL REVIEWS

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Die Konfigurationsspezifität der Lipase des Samens von Chelidonium majus. 2. Mitteilung: Über asymmetrische Ester‐Hydrolyse durch pflanzliche Enzyme

Bamann

Ullmann

1959

Archiv der Pharmazie

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Bei der Einwirkung derSarnenlipme vonChetidonium majus auf rae. MavtdekiZukemethylester treten Besonderheiten auf, die sich zunrlchst in a h bisher erarbeitete Bild iiber die ,,Konfigurationsspez@it der esterspaltmden Enzyme" nicht einzufiigen scheinen. Eine reaktionskinetische Behandlung deckt den starken E i n f l u j des Spaltungsproduktes Mardelsaure auf ulzd zeigt, &$ die neu hinzu gekommenen Erscheinungen irn Bereich &r Vielfalt &r Niiglichbikn ¥, in welcher sich die stereochemisehe Spezifitat darbieten kann. Bei der g l e i c h e e i t i g e n Einwirkung von Pankreaslipase und Leberestme (des Menschen) auf rac. MandeMureilthylester aind allerdigs eine Erhohung der [a]-Werte mit steigendem Spaltungsgmd sowie eine Abhilngigkeit des [a]-Wertes von der Zeitdauer, *) Meinem verehrten Wkultiltskollegen Herrn F'rofessor Dr., Dr. h. c. Georg-aaka Schwab in sufrichtiger Verbundenheit gewidmet a&Blich seines 60. Geburtdages. 1) 1. Wtteilung: 1. Bamnn, E . Ullmnn, A . Schuegraf und R. Bmisart, Biochem. 2. 325, 170 (1953/64).

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Das optische Auswählen der Leberesterase im System der „Ausgleichungsaktivatoren“. [IX. Mitteilung „Über asymmetrische Esterhydrolyse durch Enzyme.“]

Cited by 9 publications

References 0 publications

Quantitative Estimation of Lyo- And Desmoenzymes in Tissue Sections With and Without Fixation

Quantitative Estimation of Lyo- And Desmoenzymes in Tissue Sections With and Without Fixation

Nonoxidative Nonproteolytic Enzymes

Die Konfigurationsspezifität der Lipase des Samens von Chelidonium majus. 2. Mitteilung: Über asymmetrische Ester‐Hydrolyse durch pflanzliche Enzyme

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