Isolation and Properties of L-Asparaginases from<i>Escherichia coli</i>

Arens, A; Rauenbusch, Erich; Irion, E; Wagner, Otto; Bauer, Klaus; Kaufmann, W.

doi:10.1515/bchm2.1970.351.1.197

Cited by 58 publications

(27 citation statements)

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“…Five different active forms were seen, with their distribution fitting a Gaussian curve, as would be expected if the four subunits within 195 a form were identical. Since two asparaginases are not found in the same strain, according to Laboureur et al (86), the E. coli asparaginases cannot be isozymes, as proposed by Arens et al (35) (see section 1V.C). The results of the two groups may be reconciled by considering another observation by Laboureur having to do with "evolved" forms that appear during purification or upon standing; Laboureur et al (86) found that a series of enzymes of increasing electronegativity slowly appears.…”

Section: B Molecular Weight Shape and Subunitsmentioning

confidence: 92%

“…In aqueous solutions with a high ionic strength (e.g., 5 M NaC1) E. coli asparaginase can be dissociated into a species with an approximate molecular weight of 65,000 (88), but the observation by Kirschbaum et al (89) that the molecule is dissociated by simple dilution into a species corresponding in its molecular weight to a subunit has not been confirmed. Arens et al (35,87) did note partial dissociation upon dilution, however.…”

Section: B Molecular Weight Shape and Subunitsmentioning

confidence: 95%

“…Thus the results mentioned earlier on the N-and C-terminal amino acids (leucine only, for the nitrogen terminus, and tyrosine for the carbon terminus) suggest identical subunits. Furthermore, the Bayer group determined the sequence of the first ten amino acids at the N-terminal end, using Edman's procedure (35). They found that asparaginases A and B are identical in this region, and also that only a single amino acid was released in each application of the Edman procedure to either enzyme.…”

Section: Subunit Identitymentioning

confidence: 99%

“…The main evidence for the subunits being nonidentical comes from the experiments of Arens et al (35) using cellulose acetate strip electrophoresis. At pH 7.8 at an ionic strength of 0.1, the mobilities of asparaginases A and B are different, asparaginase B being more acidic.…”

Section: Subunit Identitymentioning

confidence: 99%

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L‐Asparaginase: A Review

Wriston¹,

Yellin²

1973

Advances in Enzymology - And Related Areas of Molecular Biology

144

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Section: B Molecular Weight Shape and Subunitsmentioning

confidence: 92%

Section: B Molecular Weight Shape and Subunitsmentioning

confidence: 95%

Section: Subunit Identitymentioning

confidence: 99%

Section: Subunit Identitymentioning

confidence: 99%

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L‐Asparaginase: A Review

Wriston¹,

Yellin²

1973

Advances in Enzymology - And Related Areas of Molecular Biology

144

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“…Asnase (E. C. 3.5.1.1): Crasnitin® (*) = Asnase A from E. coli (10) Tris-(hydroxymethyl-)aminomethane (" Tris ") from Boehringer-Mannheim (15326).…”

Section: B) Enzymes and Coenzymesmentioning

confidence: 99%

The behavior of L-asparaginase and L-asparagine in whole mice after asparaginase-application

Puetter

Flenker

1976

European Journal of Drug Metabolism and Pharmacokinetics

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Healthy mice were treared intravenously with the antileukemic L-asparaginase A by a single injection of 5,000 U/kg. At various times after injection the L-asparaginase (Asnase) content was determined in the blood-plasma and in the whole body; furthermore the simultaneous content of L-asparagine (Asn) was determined in the whole animal.Methods are described for the determination of Asnase and Asn in whole mice. The Asnase activity in the blood-plasma decreased rapidly during the first 4 hours after application. Afterwards an equilibrium of distribution was apparently reached, and the further decrease followed first order kinetics with a half-life of 3 h approximately.In the whole animal, the Asnase decrease followed from the beginning first order kinetics with a half-time of 3 h. After reaching the equilibrium, the relative volume of distribution was approximately 0.1 I/kg.In untreated mice the mean total Asn content was 26 nmoles per g. After Asnase application Asn fell, in just over one hour, below the detection limit. After two days it began to reincrease slowly; only after several days the initial value was found.The experiments have shown that Asnase also exhibits its effect apart from the circulation. It is concluded that the disturbance of the blood-mediated Asn supply is not the essential effect on sensitive cells. The problem of Asnase distribution and its influence on sensitive and resistant cells is discussed with regard to the reported results.

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Träger‐gebundene, biologisch aktive Substanzen und ihre Anwendung

Orth¹,

Brümmer²

1972

Angewandte Chemie

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Durch Bindung von Enzymen an geeignete Träger lassen sich stabile Katalysatoren gewinnen. Es werden die wichtigsten Methoden ihrer Herstellung sowie ihre Eigenschaften erläutert. Besonders interessant erscheint die Anwendung träger‐gebundener Enzyme in der biochemischen Routineanalytik als „unlösliche Reagentien”︁ für Analysenautomaten und für Enzymelektroden. Für präparative Stoffumwandlungen und Synthesen bieten die träger‐gebundenen Enzyme den Vorteil, die bisher meist diskontinuierlichen Prozesse in kontinuierliche umwandeln und proteinfreie Reaktionsprodukte erhalten zu können. Durch Verwendung träger‐gebundener Proteasen als spezifische Adsorbentien läßt sich eine Reihe natürlich vorkommender Inhibitoren in einfacher Weise isolieren. Dieses Prinzip, das der Affinitätschromatographie zugrunde liegt, wird heute umgekehrt auch zur Reinigung von Enzymen und anderen biologisch aktiven Substanzen an entsprechenden träger‐gebundenen Effektoren ausgenutzt.

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Isolation and Properties of L-Asparaginases fromEscherichia coli

Cited by 58 publications

References 0 publications

L‐Asparaginase: A Review

L‐Asparaginase: A Review

The behavior of L-asparaginase and L-asparagine in whole mice after asparaginase-application

Träger‐gebundene, biologisch aktive Substanzen und ihre Anwendung

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