<scp>l</scp>-Asparaginase from<i>E. coli</i>

Nakamura, Nobuo; Morikawa, Yasushi; Fujio, Tatsuro; Tanaka, Masao

doi:10.1080/00021369.1971.10859899

Cited by 8 publications

(9 citation statements)

References 1 publication

(1 reference statement)

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“…AC 282/309 and AC 311/321 were in-CN-7 suggests that CN-7 is a C-terminal peptide soluble in 0.05M pyridine acetate buffer (pH 3.1) of the protein. This suggestion was confirmed by 10 20 30 Leu-Pro-Asn-Ile-Thr-Ile-Leu-Ala-Thr-Gly-Gly-Thr-Ile-Ala-Gly-Gly-Gly-Asp-Ser-Ala-Thr-Lys-Ser-Asn-Tyr-Thr-Ala-Gly-Lys-Val- (CN-6), because the sequences of the methionine-containing tryptic peptides from the carboxymethylated protein (T-5, T-6, T-7, T-8 and T-10) were already established as described in the previous paperl 3 !. This alignment is shown in Fig.…”

Section: Sequence Analyses Of the Cyanogen Bromide Peptidessupporting

confidence: 71%

The Primary Structure of L-Asparaginase fromEscherichia coli

Maita¹,

Matsuda²

1980

Hoppe-Seyler´s Zeitschrift für physiologische Chemie

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The carboxymethylated L-asparagitrypsin, chymotrypsin and pepsin, and the Dansyl nase from Escherichia coli A-l -3 was fragmented Edman method. Based on the above results and with cyanogen bromide and the resulting peptides the complete sequences of the tryptic peptides were isolated by using gel filtration on Sephadex from the carboxymethylated L-asparaginase re-G-50 and column chromatography on DE-52. The ported in the previous paper, the whole sequence amino acid sequences of the 7 cyanogen bromide of the enzyme was established. The reported peptides thus obtained were established comsequence consists of 321 amino acid residues and pletely or partially by further fragmentation with its calculated molecular weight is 34080. Die Primärstruktur der L-Asparaginase von Escherichia coliZusammenfassung: Die carboxymethylierte Aufgrund dieser Ergebnisse und der Sequenzen L-Asparaginase von Escherichia coli A-l-3 wurder tryptischen Peptide der carboxymethylierten de mit Bromcyan gespalten und die erhaltenen L-Asparaginase, die in einer früheren Arbeit bePeptide wurden durch Gelfiltration an Sephadex schrieben sind, konnte die vollständige Sequenz G-50 und Säulenchromatographie an DE-52 isodes Enzyms angegeben werden. Sie besteht aus liert. Durch weitere Spaltung mittels Trypsin, 321 Aminosäureresten und hat ein berechnetes Chymotrypsin, Pepsin und die Dansyl-EdmanMolekulargewicht von 34080. Methode wurden die Aminosäuresequenzen von 7 Bromcyanpeptiden teilweise oder vollständig bestimmt.

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Section: Sequence Analyses Of the Cyanogen Bromide Peptidessupporting

confidence: 71%

The Primary Structure of L-Asparaginase fromEscherichia coli

Maita¹,

Matsuda²

1980

Hoppe-Seyler´s Zeitschrift für physiologische Chemie

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“…In literature, most described crystallization applications use L-asparaginase B purified by chromatography. Chromatography results in high purity and quality of L-asparaginase B solution and crystals [1,3,17]. Likewise, L-asparaginase B crystals were obtained based on conditions by Wagner [4] and Born and Bauer [16], i.e., 17 % of 50% PEG 6000 were mixed in the clear L-asparaginase B solution.…”

Section: Resultsmentioning

confidence: 99%

Recombinant L‐Asparaginase B and its Crystallization – What is the Nature of Protein Crystals?

Müller¹,

Liu²,

Migge³

et al. 2011

Chem Eng & Technol

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L-Asparaginase is a protein produced by Escherichia coli and exists in two types, A and B. Only type B shows a specific antitumor activity to acute lymphatic leukemia. A new recombinant E. coli BL21Gold (DE3) pET11a-ansB was used to produce L-asparaginase B in higher quantities. To enhance the purity and preserve the activity of L-asparaginase B, crystallization is a promising process. Based on available patents, first experiments on L-asparaginase B crystallization were performed. Recombinant L-asparaginase B was successfully and reproducibly crystallized in two modifications. Up to now, it is not clear in which respect these two modifications of crystalline L-asparaginase B differ. It is part of the current study to investigate the nature of protein crystals in detail. The investigations on lysozyme crystals are well in agreement with the literature.

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“…Consequently, the effects of L-asparagine 5 ) in the protection against inactivation and in the profiles of the DEAE cellulose chromatography could be attributed to L-aspartate which was formed from the added L-asparagine during the treatment. These protective actions of L-aspartate were also observed with the enzymes from Serratia marcesens12 I and Proteus vulgaris 13 I and appeared to be common to microbial L-asparaginases (EC 2).…”

Section: On the Mode Of Interaction Between L-asparaginase And L-aspamentioning

confidence: 94%

“…(4) L-Aspartate did not prevent the enzyme either from the dissociation into subunits or from decrease in the activity by urea. (5) High concentration of L-aspartate was shown to inhibit the L-asparagine hydrolysis reaction. (6) L-Aspartate was suggested from ORD measurements to cause changes in the higher structure as well as the ionic properties or proteolytic inactivation.…”

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confidence: 99%