The extracellular acid phosphatase of the mosquito-parasitizing fungus Lagenidium giganteum
The mosquito-parasitizing fungus Lagenidium giganteum secreted a soluble acid phosphatase and β- d-glucosidase into the growth medium. The acid phosphatase was isolated and purified to single component, and some of its physicochemical properties were determined. The enzyme exhibited a pH optimum of...
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| Veröffentlicht in: | Journal of invertebrate pathology 1989-11, Vol.54 (3), p.306-313 |
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| container_title | Journal of invertebrate pathology |
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| creator | Bell, T.J. Lee, B. Domnas, A.J. |
| description | The mosquito-parasitizing fungus
Lagenidium giganteum secreted a soluble acid phosphatase and β-
d-glucosidase into the growth medium. The acid phosphatase was isolated and purified to single component, and some of its physicochemical properties were determined. The enzyme exhibited a
pH optimum of 5.6 in phthalate buffer with
p-nitrophenyl phosphate and was temperature-inactivated at 55°C. Enzyme activity seems to be limited to phenyl-phosphate substrates. A molecular weight of 42,800 was found and the amino acid content was also determined. A
K
m
for
p-nitrophenyl phosphate of 1.6 × 10
−7
m was found. The possible involvement of the enzyme in the infective process was discussed. |
| doi_str_mv | 10.1016/0022-2011(89)90114-6 |
| format | Article |
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Lagenidium giganteum secreted a soluble acid phosphatase and β-
d-glucosidase into the growth medium. The acid phosphatase was isolated and purified to single component, and some of its physicochemical properties were determined. The enzyme exhibited a
pH optimum of 5.6 in phthalate buffer with
p-nitrophenyl phosphate and was temperature-inactivated at 55°C. Enzyme activity seems to be limited to phenyl-phosphate substrates. A molecular weight of 42,800 was found and the amino acid content was also determined. A
K
m
for
p-nitrophenyl phosphate of 1.6 × 10
−7
m was found. The possible involvement of the enzyme in the infective process was discussed.</description><identifier>ISSN: 0022-2011</identifier><identifier>EISSN: 1096-0805</identifier><identifier>DOI: 10.1016/0022-2011(89)90114-6</identifier><identifier>PMID: 2572649</identifier><identifier>CODEN: JIVPAZ</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>ACID PHOSPHATASE ; Acid Phosphatase - antagonists & inhibitors ; Acid Phosphatase - metabolism ; Amino Acids - analysis ; Animals ; Biological and medical sciences ; Cell biochemistry ; Cell physiology ; CHAMPIGNON ENTOMOGENE ; Chytridiomycota - enzymology ; CONTROL DE PLAGAS ; Culicidae ; Culicidae - microbiology ; DIPTERA ; ENTOMOGENOUS FUNGI ; enzymes ; EPURATION ; exocellular acid phosphatase ; FOSFATASA ACIDA ; Fundamental and applied biological sciences. Psychology ; HONGOS ENTOMOGENOS ; Insecta ; INSECTE NUISIBLE ; INSECTOS DANINOS ; Invertebrates ; Kinetics ; Lagenidium giganteum ; LUTTE ANTI-PARASITE ; Oomycetes - enzymology ; PARASITE ; PARASITES ; PARASITOS ; PATHOGENICITY ; Pathology ; PEST CONTROL ; PEST INSECTS ; PHOSPHATASE ACIDE ; Plant physiology and development ; PODER PATOGENO ; POUVOIR PATHOGENE ; PURIFICACION ; PURIFICATION ; Substrate Specificity</subject><ispartof>Journal of invertebrate pathology, 1989-11, Vol.54 (3), p.306-313</ispartof><rights>1989</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c436t-2a6fb924a35f008f0e6fd2cb29361c6dc40c91421b42c6383f231905819b561c3</citedby><cites>FETCH-LOGICAL-c436t-2a6fb924a35f008f0e6fd2cb29361c6dc40c91421b42c6383f231905819b561c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0022-2011(89)90114-6$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6840043$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2572649$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bell, T.J.</creatorcontrib><creatorcontrib>Lee, B.</creatorcontrib><creatorcontrib>Domnas, A.J.</creatorcontrib><title>The extracellular acid phosphatase of the mosquito-parasitizing fungus Lagenidium giganteum</title><title>Journal of invertebrate pathology</title><addtitle>J Invertebr Pathol</addtitle><description>The mosquito-parasitizing fungus
Lagenidium giganteum secreted a soluble acid phosphatase and β-
d-glucosidase into the growth medium. The acid phosphatase was isolated and purified to single component, and some of its physicochemical properties were determined. The enzyme exhibited a
pH optimum of 5.6 in phthalate buffer with
p-nitrophenyl phosphate and was temperature-inactivated at 55°C. Enzyme activity seems to be limited to phenyl-phosphate substrates. A molecular weight of 42,800 was found and the amino acid content was also determined. A
K
m
for
p-nitrophenyl phosphate of 1.6 × 10
−7
m was found. The possible involvement of the enzyme in the infective process was discussed.</description><subject>ACID PHOSPHATASE</subject><subject>Acid Phosphatase - antagonists & inhibitors</subject><subject>Acid Phosphatase - metabolism</subject><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell biochemistry</subject><subject>Cell physiology</subject><subject>CHAMPIGNON ENTOMOGENE</subject><subject>Chytridiomycota - enzymology</subject><subject>CONTROL DE PLAGAS</subject><subject>Culicidae</subject><subject>Culicidae - microbiology</subject><subject>DIPTERA</subject><subject>ENTOMOGENOUS FUNGI</subject><subject>enzymes</subject><subject>EPURATION</subject><subject>exocellular acid phosphatase</subject><subject>FOSFATASA ACIDA</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HONGOS ENTOMOGENOS</subject><subject>Insecta</subject><subject>INSECTE NUISIBLE</subject><subject>INSECTOS DANINOS</subject><subject>Invertebrates</subject><subject>Kinetics</subject><subject>Lagenidium giganteum</subject><subject>LUTTE ANTI-PARASITE</subject><subject>Oomycetes - enzymology</subject><subject>PARASITE</subject><subject>PARASITES</subject><subject>PARASITOS</subject><subject>PATHOGENICITY</subject><subject>Pathology</subject><subject>PEST CONTROL</subject><subject>PEST INSECTS</subject><subject>PHOSPHATASE ACIDE</subject><subject>Plant physiology and development</subject><subject>PODER PATOGENO</subject><subject>POUVOIR PATHOGENE</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>Substrate Specificity</subject><issn>0022-2011</issn><issn>1096-0805</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE2LFDEQhoMo67j6B0ShDyJ6aK2k0-nOZUEWv2DAg7snD6E6nfRE-mvzIeqvN-0Mc9RTFbxPVSUPIc8ovKFAxVsAxkoGlL5q5WuZKy_FPbKjIEUJLdT3ye6MPCSPQvgOuauFvCAXrG6Y4HJHvt0cTGF-Ro_ajGMa0ReoXV-shyWsB4wYTLHYImZqWsJdcnEpV_QYXHS_3TwUNs1DCsUeBzO73qWpGNyAczRpekweWByDeXKql-T2w_ub60_l_svHz9fv9qXmlYglQ2E7yThWtQVoLRhhe6Y7JitBteg1By0pZ7TjTIuqrSyrqIS6pbKrM1FdkpfHvatf7pIJUU0ubN_B2SwpqEYyyRoB_wVpzXlTNyKD_Ahqv4TgjVWrdxP6X4qC2uSrzazazKpWqr_y1Tb2_LQ_dZPpz0Mn2zl_ccoxaBytx1m7cMZEywF4lbGnR8zionDwGbn9mm8I2tIcXh1Dk43-cMaroJ2ZtemdNzqqfnH_fuQfpbGoCw</recordid><startdate>19891101</startdate><enddate>19891101</enddate><creator>Bell, T.J.</creator><creator>Lee, B.</creator><creator>Domnas, A.J.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19891101</creationdate><title>The extracellular acid phosphatase of the mosquito-parasitizing fungus Lagenidium giganteum</title><author>Bell, T.J. ; Lee, B. ; Domnas, A.J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c436t-2a6fb924a35f008f0e6fd2cb29361c6dc40c91421b42c6383f231905819b561c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>ACID PHOSPHATASE</topic><topic>Acid Phosphatase - antagonists & inhibitors</topic><topic>Acid Phosphatase - metabolism</topic><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell biochemistry</topic><topic>Cell physiology</topic><topic>CHAMPIGNON ENTOMOGENE</topic><topic>Chytridiomycota - enzymology</topic><topic>CONTROL DE PLAGAS</topic><topic>Culicidae</topic><topic>Culicidae - microbiology</topic><topic>DIPTERA</topic><topic>ENTOMOGENOUS FUNGI</topic><topic>enzymes</topic><topic>EPURATION</topic><topic>exocellular acid phosphatase</topic><topic>FOSFATASA ACIDA</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>HONGOS ENTOMOGENOS</topic><topic>Insecta</topic><topic>INSECTE NUISIBLE</topic><topic>INSECTOS DANINOS</topic><topic>Invertebrates</topic><topic>Kinetics</topic><topic>Lagenidium giganteum</topic><topic>LUTTE ANTI-PARASITE</topic><topic>Oomycetes - enzymology</topic><topic>PARASITE</topic><topic>PARASITES</topic><topic>PARASITOS</topic><topic>PATHOGENICITY</topic><topic>Pathology</topic><topic>PEST CONTROL</topic><topic>PEST INSECTS</topic><topic>PHOSPHATASE ACIDE</topic><topic>Plant physiology and development</topic><topic>PODER PATOGENO</topic><topic>POUVOIR PATHOGENE</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bell, T.J.</creatorcontrib><creatorcontrib>Lee, B.</creatorcontrib><creatorcontrib>Domnas, A.J.</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of invertebrate pathology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bell, T.J.</au><au>Lee, B.</au><au>Domnas, A.J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The extracellular acid phosphatase of the mosquito-parasitizing fungus Lagenidium giganteum</atitle><jtitle>Journal of invertebrate pathology</jtitle><addtitle>J Invertebr Pathol</addtitle><date>1989-11-01</date><risdate>1989</risdate><volume>54</volume><issue>3</issue><spage>306</spage><epage>313</epage><pages>306-313</pages><issn>0022-2011</issn><eissn>1096-0805</eissn><coden>JIVPAZ</coden><abstract>The mosquito-parasitizing fungus
Lagenidium giganteum secreted a soluble acid phosphatase and β-
d-glucosidase into the growth medium. The acid phosphatase was isolated and purified to single component, and some of its physicochemical properties were determined. The enzyme exhibited a
pH optimum of 5.6 in phthalate buffer with
p-nitrophenyl phosphate and was temperature-inactivated at 55°C. Enzyme activity seems to be limited to phenyl-phosphate substrates. A molecular weight of 42,800 was found and the amino acid content was also determined. A
K
m
for
p-nitrophenyl phosphate of 1.6 × 10
−7
m was found. The possible involvement of the enzyme in the infective process was discussed.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><pmid>2572649</pmid><doi>10.1016/0022-2011(89)90114-6</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Journal of invertebrate pathology, 1989-11, Vol.54 (3), p.306-313 |
| issn | 0022-2011 1096-0805 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | ACID PHOSPHATASE Acid Phosphatase - antagonists & inhibitors Acid Phosphatase - metabolism Amino Acids - analysis Animals Biological and medical sciences Cell biochemistry Cell physiology CHAMPIGNON ENTOMOGENE Chytridiomycota - enzymology CONTROL DE PLAGAS Culicidae Culicidae - microbiology DIPTERA ENTOMOGENOUS FUNGI enzymes EPURATION exocellular acid phosphatase FOSFATASA ACIDA Fundamental and applied biological sciences. Psychology HONGOS ENTOMOGENOS Insecta INSECTE NUISIBLE INSECTOS DANINOS Invertebrates Kinetics Lagenidium giganteum LUTTE ANTI-PARASITE Oomycetes - enzymology PARASITE PARASITES PARASITOS PATHOGENICITY Pathology PEST CONTROL PEST INSECTS PHOSPHATASE ACIDE Plant physiology and development PODER PATOGENO POUVOIR PATHOGENE PURIFICACION PURIFICATION Substrate Specificity |
| title | The extracellular acid phosphatase of the mosquito-parasitizing fungus Lagenidium giganteum |
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