Partial purification and antilymphoma activity of Serratia marcescensL-asparaginase

Rowley, Barbara; Wriston, John C.

doi:10.1016/0006-291x(67)90423-8

Cited by 52 publications

(15 citation statements)

References 7 publications

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“…Several researchers have studied the isolation of microbial strains that produce this important enzyme, such as Pseudomonas fluorescens , 32 Serratia marcescens , 33 Escherichia coli , 34 Erwinia carotovora , 35 Proteus vulgaris , 36 Saccharomyces cerevisiae , Karnatakensis Streptomyces, Streptomyces venezuelae and several genres of fungi as Aspergillus, Penicillium and Fusarium 37 …”

Section: L-asparaginase Applicationsmentioning

confidence: 99%

Current applications and different approaches for microbial l-asparaginase production

Cachumba

Antunes

Peres

et al. 2016

Brazilian Journal of Microbiology

173

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l-asparaginase (EC 3.5.1.1) is an enzyme that catalysis mainly the asparagine hydrolysis in l-aspartic acid and ammonium. This enzyme is presented in different organisms, such as microorganisms, vegetal, and some animals, including certain rodent's serum, but not unveiled in humans. It can be used as important chemotherapeutic agent for the treatment of a variety of lymphoproliferative disorders and lymphomas (particularly acute lymphoblastic leukemia (ALL) and Hodgkin's lymphoma), and has been a pivotal agent in chemotherapy protocols from around 30 years. Also, other important application is in food industry, by using the properties of this enzyme to reduce acrylamide levels in commercial fried foods, maintaining their characteristics (color, flavor, texture, security, etc.) Actually, l-asparaginase catalyzes the hydrolysis of l-asparagine, not allowing the reaction of reducing sugars with this aminoacid for the generation of acrylamide. Currently, production of l-asparaginase is mainly based in biotechnological production by using some bacteria. However, industrial production also needs research work aiming to obtain better production yields, as well as novel process by applying different microorganisms to increase the range of applications of the produced enzyme. Within this context, this mini-review presents l-asparaginase applications, production by different microorganisms and some limitations, current investigations, as well as some challenges to be achieved for profitable industrial production.

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Section: L-asparaginase Applicationsmentioning

confidence: 99%

Current applications and different approaches for microbial l-asparaginase production

Cachumba

Antunes

Peres

et al. 2016

Brazilian Journal of Microbiology

173

View full text Add to dashboard Cite

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“…coli, produced a very potent preparation, one indeed which in relation to asparaginase assay was a more effective tumor inhibitor than guinea pig serum.21 Recently, 3 further tumor inhibitory asparaginase has been obtained by Rowley and Wriston from S. marcessens. 22 The E . coli asparaginase preparations have been shown by others and by us to consist of two enzymes.23-25 Using preparations derived from strain K-12, Schwartz, Reeve, and I have shown that the two enzymes differ in a number of properties, but one which appears to be of particular significance is in their avidity for asparagine.24 E .…”

Section: Effects Of Asparaginases From Other Sources On Tumorsmentioning

confidence: 99%

DIVISION OF MICROBIOLOGY: L‐ASPARAGINASE: THE EVOLUTION OF A NEW TUMOR INHIBITORY AGENT*

Broome

1968

Trans NY Acad Sci

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All accounts of the finding that L-asparaginases have tumor inhibitory properties must begin in the same way: with the observations of Kidd, r eported in 1953, that when normal guinea pig serum is injected into mice and rats bearing certain transplanted lymphomas a striking regression, even of established tumors, was produced.1,a This significant discovery was made during the course of studies in which the serum was used as a source of complement in an attempt to enhance the activity of heterologous antiserum made against the tumor. The combination of guinea pig serum and antibody was highly effective, but a strong tumor inhibitory activity was found in controls given guinea pig serum alone. From this beginning Kidd established a number of fundamental points about the activity of guinea pig serum which, although now subjected to reexamination on a larger scale, remain essentially unmodified. First, he showed that tumor inhibition was produced only by guinea pig serum; s e r a of several other species, namely, the horse, the rabbit, and the human, were without effect. Secondly, he showed that although three different lymphomas, 6C3HED and Lorenz's Lymphoma 2 in mice, and the Murphy-Sturm lymphosarcoma of rats were highly sensitive, and with the first two complete regression of large established tumors could be regularly obtained, others were totally insensitive. Indeed, later work with 20 different lymphomas, most of them recently induced, did not reveal a single sensitive line.3 Thirdly, it was found that animals treated with guinea pig serum in doses which completely inhibited their tumors, o r even over prolonged periods with larger amounts, were not made toxic. The animals appeared in every way normal, and gross and microscopic examination of their tissues revealed no pathological changes.Because of the way in which the discovery was made and because at f i r s t it appeared that only long transplanted tumors were sensitive, guinea pig serum was generally thought to act through its high complementary activity, in augmenting an immunological reaction between the host and the implanted tumor, Kidd, I believe, was never convinced of this explanation and a number of findings were hard to reconcile with it.

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“…Asparaginase from this strain is synthesized in greatest quantities when cells are grown aerobically in the presence of glutamic acid, methionine, and lactic acid. Glucose represses the synthesis of the enzyme, Asparaginases in many other species of bacteria have also been examined (64,77,82,89,90,96,104 i.…”

Section: -6-mentioning

confidence: 99%

L-Asparagine degradation in saccharomyces cerevisiae: Genetic control and biochemical properties of yeast L-asparaginase

Jones¹

1970

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Partial purification and antilymphoma activity of Serratia marcescensL-asparaginase

Cited by 52 publications

References 7 publications

Current applications and different approaches for microbial l-asparaginase production

Current applications and different approaches for microbial l-asparaginase production

DIVISION OF MICROBIOLOGY: L‐ASPARAGINASE: THE EVOLUTION OF A NEW TUMOR INHIBITORY AGENT*

L-Asparagine degradation in saccharomyces cerevisiae: Genetic control and biochemical properties of yeast L-asparaginase

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