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Analysis of Leishmania proteinases reveals developmental changes in species-specific forms and a common 68-kDa activity (1987)

Lockwood, Barbara C. ; North, Michael J. ; Mallinson, David J. ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

FEMS microbiology letters 48 (1987), S. 0

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ISSN: 1574-6968

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology

Notes: Abstract The proteinases of three species of Leishmania have been analysed by electrophoresis. Amastigotes of L. mexicana mexicana have several high-activity, low-Mr cysteine proteinases which are absent from log-phase promastigotes of L. m. mexicana and from all developmental stages of the other species analysed (L. donovani and L. major). Low-activity, low-Mr proteinases were present in populations of stationary-phase promastigotes of L. m. mexicana. All three species of Leishmania had higher Mr proteinases, a number of which showed developmental regulation, some of them being stage-specific. Significantly, at all stages of the life cycle in all three species a 68-kDa proteinase was apparent. In its size, sensitivity to inhibitors and ability to bind concanavalin A-agarose, this resembles the major surface protein thought to be present in all Leishmania species and which has recently been reported to possess proteinase activity in L. major promastigotes.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1574-6968.1987.tb02622.x

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Purine-metabolizing enzymes in Babesia divergens (1987)

Hassan, Husain F. ; Phillips, R. Stephen ; Coombs, Graham H.

Springer

Parasitology research 73 (1987), S. 121-125

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ISSN: 1432-1955

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Abstract Extracts of Babesia divergens were examined for the enzymes which catalyse purine salvage. Adenosine deaminase (EC 3.5.4.4), guanine deaminase (EC 3.5.4.3), inosine phosphorylase (EC 2.4.2.1), purine phosphoribosyltransferases (EC 2.4.2.7, EC 2.4.2.8, EC 2.4.2.22) and nucleoside kinases (EC 2.7.1.15, EC 2.7.1.20, EC 2.7.1.73) were all detected at relatively high activities, whereas nucleotide interconverting enzymes were not detected. Coformycin and 4-amino-5-imidazolecarboxamide were found to be potent inhibitors of adenosine deaminase and guanine deaminase, respectively. The results suggest that B. divergens is capable of synthesizing purine nucleotides via two routes, one involving purine phosphoribosyltransferases and the other employing nucleoside kinases.