Einwirkung von Cyankalium auf aliphatische Aldehyde

Kohn, Leopold

doi:10.1007/bf01524678

Cited by 7 publications

(2 citation statements)

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“…A role for CAF in metabolic turnover of myofibrils is supported by our preliminary results showing that CAF activity is elevated in atrophying denervated muscle (Jergenson, Robson, and Stromer, unpublished results) and in muscle from dystrophic chickens (Reville and Zeece, unpublished results). Furthermore, Kohn (1969) found that activity of his soluble proteolytic fraction increased significantly in atrophying rat skeletal muscle, and, as indicated earlier, it is very likely that Kohn's soluble proteolytic fraction contained CAF. Several studies (Issacson and Sandow, 1968;Varley and Dhalla, 1973;Vihert and Pozdyunina, 1969;Young etal., 1959) have shown that intracellular free Ca2+ levels increase during pathological or necrotic states in muscle cells, and it is possible that this increase in free Ca2+ concentration is sufficient to activate CAF, which may then initiate myofibrillar degeneration.…”

Section: Discussionsupporting

confidence: 61%

“…Consequently, the available data indicate that CAF is an intracellular proteolytic enzyme located in the sarcoplasm of muscle cells. It seems probable that CAF was one of the active enzymes in a crude muscle enzyme fraction isolated in 1969 by Kohn (1969), and as discussed in the preceding paper (Dayton et al, 1976b), it is very likely that CAF is identical with the kinaseactivating factor that was purified to 60% homogeneity by Huston and Krebs (1968). The data in this paper show that CAF is optimally active under conditions of pH and temperature that exist in the sarcoplasm of normal, living muscle cells in vivo, and because CAF seems to be located in the sarcoplasm, it is imperative that CAF activity be closely regulated in some way to prevent continuous and indiscriminate degradation of myofibrils in living cells.…”

Section: Discussionmentioning

confidence: 99%

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A calcium(2+) ion-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme

Dayton¹,

Reville²,

Goll³

et al. 1976

Biochemistry

390

116

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The purified Ca2+-activated protease (CAF) isolated from porcine skeletal muscle and capable of removing Z-disks from intact myofibrils is optimally active on either myofibril or casein substrates at pH 7.5 and in the presence of 1 mM Ca2+ and at least 2 mM 2-mercaptoethanol. No CAF activity is detected when 1 mM Mg2+, Mn2+, Ba2+, Co2+, Ni2+, and Fe2+ are added singly. When added with 1 mM Ca2+, Co2+, Cu2+, Ni2+, and Fe2+ inhibit, whereas Mg2+, Mn2+, and Ba2+ have no effect on CAF activity. CAF is irreversibly inhibited by iodoacetate but is unaffected by soybean trypsin inhibitor. S0/20,W=5.90 S, and sedimentation equilibrium molecular weight - 112 000 for purified CAF. Because purified CAF migrates as two polypeptide chains with molecular weights of 80 000 and 30 000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the CAF molecule must consist of one each of these two polypeptide chains. Approximate molecular dimensions of 38 X 220 A can be calculated for CAF from calibrated gel permeation column data or from S0/20,W and the molecular weight. Amino acid composition and physical properties of purified CAF distinguish it from the known catheptic enzymes and from other proteases found in blood or in granulocytes. Purified CAF removes Z-disks the 400-A periodicity associated with troponin in the I band and partly degrades M lines but causes no other ultrastructurally detectable effects when incubated with myofibrils. These results agree with the earlier finding that purified CAF degrades troponin, tropomyosin, and C-protein but has no effect on myosin, actin, or alpha-actinin, and suggest that CAF may have a physiological role in disassembly of intact myofibrils during metabolic turnover of myofibrillar proteins.

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Section: Discussionsupporting

confidence: 61%

Section: Discussionmentioning

confidence: 99%

A calcium(2+) ion-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme

Dayton¹,

Reville²,

Goll³

et al. 1976

Biochemistry

390

116

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Ueber die Einwirkung von Alkali‐ und Erdalkalicyaniden auf Traubenzucker

Rupp¹,

Hölzle²

1913

Archiv der Pharmazie

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Die Kinetik der Reaktionen polymerer Aldehyde, II. Mitteil.: Die Reaktion von Paraformaldehyd mit Cyanid

Löbering

Jung

1936

Ber. dtsch. Chem. Ges. A/B

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1936)l Lobering, Jung. 2147 wurde das Dibromid I1 vom Schmp. 162O erhalten; der Mischschmp. mit dem aus Cholestenon erhaltenen Dibromid I1 gab keine Depression ; Ausbeute 1.1 g. K e t 0-mono b r o m i d V. Zu einer Losung von 2.2 g IV in 70 ccm Ather wurde zuerst eine Losung von 4 g Kaliumacetat in 75 ccm 85-proz. Essigsaure gegeben und darauf bei 3 O unter Rtihren eine Liisung von 0.8 g B r o m (1 Mol.) in 25 ccm Eisessig h n e i h d b von 10 Min. zugetropft. Das Brom wurde sofort aufgenommen. Dann wurde der Ather imVak. bei 35O abgedainpft bis sich die Lijsung triibte. Beim Stehenlassen schieden sich bald reichliche Mengen schoner Nadeln ab ; Absaugen und Waschen mit Alkohol. Ausbeute 1.4 g, aus der Mutterlauge durch Verdunnen mit Wasser weitere 0 . 3 -0 . 4 g. Durch Umkrystallisieren aus Alkohol erhiilt man den Stoff in prachtigen Nadeln, die, fein zerrieben, bei 132O schmelzen. 4.860 mg Sbst. : 12.430 mg CO,, 4.02 mg H,O. -14.400 mg Sbst. : 5.90 mg AgBr.

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Einwirkung von Cyankalium auf aliphatische Aldehyde

Abstract: Aus dem chemischen Laboratorium des Hofrathes Ad. Lieben an der k. k. Universit~it in Wien.) (Vorgelegt in der Sitzung am 19. October t899.

Cited by 7 publications

References 0 publications

A calcium(2+) ion-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme

A calcium(2+) ion-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme

Ueber die Einwirkung von Alkali‐ und Erdalkalicyaniden auf Traubenzucker

Die Kinetik der Reaktionen polymerer Aldehyde, II. Mitteil.: Die Reaktion von Paraformaldehyd mit Cyanid

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