Loading…

Acid Phosphatases from the Liver of Labeo rohita

Low molecular weight acid phosphatase (LM-ACP) peak 2 (the isoenzyme corresponding to isoform 2, IF-2) from the liver of fish Rahu (Labeo rohita) was purified to homogeneity. 900 times purification resulted with specific activity of 35 U/mg of protein and recovery of 0.2%. The enzyme was found homog...

Full description

Saved in:
Bibliographic Details
Published in:Biological & pharmaceutical bulletin 2008-05, Vol.31 (5), p.802
Main Authors: Siddiqua, Aisha, Rehmat, Mamoona, Saeed, Asma, Amin, Shazia, Naz, Rubina, Sherazi, Mehrin, Majeed Khan, Gul, Saeed, Ahmad
Format: Article
Language:English
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page
container_issue 5
container_start_page 802
container_title Biological & pharmaceutical bulletin
container_volume 31
creator Siddiqua, Aisha
Rehmat, Mamoona
Saeed, Asma
Amin, Shazia
Naz, Rubina
Sherazi, Mehrin
Majeed Khan, Gul
Saeed, Ahmad
description Low molecular weight acid phosphatase (LM-ACP) peak 2 (the isoenzyme corresponding to isoform 2, IF-2) from the liver of fish Rahu (Labeo rohita) was purified to homogeneity. 900 times purification resulted with specific activity of 35 U/mg of protein and recovery of 0.2%. The enzyme was found homogeneous on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Molecular weight of 18 killo Daltons (kDa) was obtained. The peak 1 isoenzyme corresponding to isoform1 (IF-1) was partially purified about 160 times with specific activity of 7 U/mg of protein. Major protein band corresponding to 18 kDa was seen along with other protein faint bands. High molecular weight acid phosphatase (HM-ACP) was also partially purified. The molecular weight was estimated to be a 100 kDa by gel filtration on Sephadex G-100. LM-ACP isoenzymes and HM-ACP enzyme were studied for their substrate specificity, sensitivity to inhibitors or activators and other kinetic parameters. LM-ACP isoenzymes were not inhibited by tartrate and fluoride but were inhibited by sulfhydryl reagent whereas high molecular weight enzyme was strongly inhibited by fluoride and tartrate. Phosphate vanadate and molybdate inhibited both types of enzymes competitively, but their action was more pronounced in HM-ACP enzyme. LM-ACP was effectively activated by purine compounds whereas HM-ACP was not. LM-ACP showed strict substrate specificity while HM-ACP showed broad substrate specificity. The two types of acid phosphatases also differed in their rate of hydrolysis of α-naphthyl phosphate and β-glyerophosphate.
format article
fullrecord <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_journals_1449369369</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3121406941</sourcerecordid><originalsourceid>FETCH-proquest_journals_14493693693</originalsourceid><addsrcrecordid>eNpjYuA0NDYx1zU1MjRlYeA0sDS00DUzNLXgYOAqLs4yMDAwNzAy5mQwcEzOTFEIyMgvLshILEksTi1WSCvKz1UoyUhV8MksSy1SyE9T8ElMSs1XKMrPyCxJ5GFgTUvMKU7lhdLcDMpuriHOHroFRfmFpanFJfFZ-aVFeUCpeEMTE0tjMzAiThUAA5kz2Q</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1449369369</pqid></control><display><type>article</type><title>Acid Phosphatases from the Liver of Labeo rohita</title><source>Free Full-Text Journals in Chemistry</source><creator>Siddiqua, Aisha ; Rehmat, Mamoona ; Saeed, Asma ; Amin, Shazia ; Naz, Rubina ; Sherazi, Mehrin ; Majeed Khan, Gul ; Saeed, Ahmad</creator><creatorcontrib>Siddiqua, Aisha ; Rehmat, Mamoona ; Saeed, Asma ; Amin, Shazia ; Naz, Rubina ; Sherazi, Mehrin ; Majeed Khan, Gul ; Saeed, Ahmad</creatorcontrib><description>Low molecular weight acid phosphatase (LM-ACP) peak 2 (the isoenzyme corresponding to isoform 2, IF-2) from the liver of fish Rahu (Labeo rohita) was purified to homogeneity. 900 times purification resulted with specific activity of 35 U/mg of protein and recovery of 0.2%. The enzyme was found homogeneous on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Molecular weight of 18 killo Daltons (kDa) was obtained. The peak 1 isoenzyme corresponding to isoform1 (IF-1) was partially purified about 160 times with specific activity of 7 U/mg of protein. Major protein band corresponding to 18 kDa was seen along with other protein faint bands. High molecular weight acid phosphatase (HM-ACP) was also partially purified. The molecular weight was estimated to be a 100 kDa by gel filtration on Sephadex G-100. LM-ACP isoenzymes and HM-ACP enzyme were studied for their substrate specificity, sensitivity to inhibitors or activators and other kinetic parameters. LM-ACP isoenzymes were not inhibited by tartrate and fluoride but were inhibited by sulfhydryl reagent whereas high molecular weight enzyme was strongly inhibited by fluoride and tartrate. Phosphate vanadate and molybdate inhibited both types of enzymes competitively, but their action was more pronounced in HM-ACP enzyme. LM-ACP was effectively activated by purine compounds whereas HM-ACP was not. LM-ACP showed strict substrate specificity while HM-ACP showed broad substrate specificity. The two types of acid phosphatases also differed in their rate of hydrolysis of α-naphthyl phosphate and β-glyerophosphate.</description><identifier>ISSN: 0918-6158</identifier><identifier>EISSN: 1347-5215</identifier><language>eng</language><publisher>Tokyo: Japan Science and Technology Agency</publisher><ispartof>Biological &amp; pharmaceutical bulletin, 2008-05, Vol.31 (5), p.802</ispartof><rights>Copyright Japan Science and Technology Agency 2008</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780</link.rule.ids></links><search><creatorcontrib>Siddiqua, Aisha</creatorcontrib><creatorcontrib>Rehmat, Mamoona</creatorcontrib><creatorcontrib>Saeed, Asma</creatorcontrib><creatorcontrib>Amin, Shazia</creatorcontrib><creatorcontrib>Naz, Rubina</creatorcontrib><creatorcontrib>Sherazi, Mehrin</creatorcontrib><creatorcontrib>Majeed Khan, Gul</creatorcontrib><creatorcontrib>Saeed, Ahmad</creatorcontrib><title>Acid Phosphatases from the Liver of Labeo rohita</title><title>Biological &amp; pharmaceutical bulletin</title><description>Low molecular weight acid phosphatase (LM-ACP) peak 2 (the isoenzyme corresponding to isoform 2, IF-2) from the liver of fish Rahu (Labeo rohita) was purified to homogeneity. 900 times purification resulted with specific activity of 35 U/mg of protein and recovery of 0.2%. The enzyme was found homogeneous on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Molecular weight of 18 killo Daltons (kDa) was obtained. The peak 1 isoenzyme corresponding to isoform1 (IF-1) was partially purified about 160 times with specific activity of 7 U/mg of protein. Major protein band corresponding to 18 kDa was seen along with other protein faint bands. High molecular weight acid phosphatase (HM-ACP) was also partially purified. The molecular weight was estimated to be a 100 kDa by gel filtration on Sephadex G-100. LM-ACP isoenzymes and HM-ACP enzyme were studied for their substrate specificity, sensitivity to inhibitors or activators and other kinetic parameters. LM-ACP isoenzymes were not inhibited by tartrate and fluoride but were inhibited by sulfhydryl reagent whereas high molecular weight enzyme was strongly inhibited by fluoride and tartrate. Phosphate vanadate and molybdate inhibited both types of enzymes competitively, but their action was more pronounced in HM-ACP enzyme. LM-ACP was effectively activated by purine compounds whereas HM-ACP was not. LM-ACP showed strict substrate specificity while HM-ACP showed broad substrate specificity. The two types of acid phosphatases also differed in their rate of hydrolysis of α-naphthyl phosphate and β-glyerophosphate.</description><issn>0918-6158</issn><issn>1347-5215</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><recordid>eNpjYuA0NDYx1zU1MjRlYeA0sDS00DUzNLXgYOAqLs4yMDAwNzAy5mQwcEzOTFEIyMgvLshILEksTi1WSCvKz1UoyUhV8MksSy1SyE9T8ElMSs1XKMrPyCxJ5GFgTUvMKU7lhdLcDMpuriHOHroFRfmFpanFJfFZ-aVFeUCpeEMTE0tjMzAiThUAA5kz2Q</recordid><startdate>20080501</startdate><enddate>20080501</enddate><creator>Siddiqua, Aisha</creator><creator>Rehmat, Mamoona</creator><creator>Saeed, Asma</creator><creator>Amin, Shazia</creator><creator>Naz, Rubina</creator><creator>Sherazi, Mehrin</creator><creator>Majeed Khan, Gul</creator><creator>Saeed, Ahmad</creator><general>Japan Science and Technology Agency</general><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope></search><sort><creationdate>20080501</creationdate><title>Acid Phosphatases from the Liver of Labeo rohita</title><author>Siddiqua, Aisha ; Rehmat, Mamoona ; Saeed, Asma ; Amin, Shazia ; Naz, Rubina ; Sherazi, Mehrin ; Majeed Khan, Gul ; Saeed, Ahmad</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-proquest_journals_14493693693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Siddiqua, Aisha</creatorcontrib><creatorcontrib>Rehmat, Mamoona</creatorcontrib><creatorcontrib>Saeed, Asma</creatorcontrib><creatorcontrib>Amin, Shazia</creatorcontrib><creatorcontrib>Naz, Rubina</creatorcontrib><creatorcontrib>Sherazi, Mehrin</creatorcontrib><creatorcontrib>Majeed Khan, Gul</creatorcontrib><creatorcontrib>Saeed, Ahmad</creatorcontrib><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Biological &amp; pharmaceutical bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Siddiqua, Aisha</au><au>Rehmat, Mamoona</au><au>Saeed, Asma</au><au>Amin, Shazia</au><au>Naz, Rubina</au><au>Sherazi, Mehrin</au><au>Majeed Khan, Gul</au><au>Saeed, Ahmad</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Acid Phosphatases from the Liver of Labeo rohita</atitle><jtitle>Biological &amp; pharmaceutical bulletin</jtitle><date>2008-05-01</date><risdate>2008</risdate><volume>31</volume><issue>5</issue><spage>802</spage><pages>802-</pages><issn>0918-6158</issn><eissn>1347-5215</eissn><abstract>Low molecular weight acid phosphatase (LM-ACP) peak 2 (the isoenzyme corresponding to isoform 2, IF-2) from the liver of fish Rahu (Labeo rohita) was purified to homogeneity. 900 times purification resulted with specific activity of 35 U/mg of protein and recovery of 0.2%. The enzyme was found homogeneous on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Molecular weight of 18 killo Daltons (kDa) was obtained. The peak 1 isoenzyme corresponding to isoform1 (IF-1) was partially purified about 160 times with specific activity of 7 U/mg of protein. Major protein band corresponding to 18 kDa was seen along with other protein faint bands. High molecular weight acid phosphatase (HM-ACP) was also partially purified. The molecular weight was estimated to be a 100 kDa by gel filtration on Sephadex G-100. LM-ACP isoenzymes and HM-ACP enzyme were studied for their substrate specificity, sensitivity to inhibitors or activators and other kinetic parameters. LM-ACP isoenzymes were not inhibited by tartrate and fluoride but were inhibited by sulfhydryl reagent whereas high molecular weight enzyme was strongly inhibited by fluoride and tartrate. Phosphate vanadate and molybdate inhibited both types of enzymes competitively, but their action was more pronounced in HM-ACP enzyme. LM-ACP was effectively activated by purine compounds whereas HM-ACP was not. LM-ACP showed strict substrate specificity while HM-ACP showed broad substrate specificity. The two types of acid phosphatases also differed in their rate of hydrolysis of α-naphthyl phosphate and β-glyerophosphate.</abstract><cop>Tokyo</cop><pub>Japan Science and Technology Agency</pub></addata></record>
fulltext fulltext
identifier ISSN: 0918-6158
ispartof Biological & pharmaceutical bulletin, 2008-05, Vol.31 (5), p.802
issn 0918-6158
1347-5215
language eng
recordid cdi_proquest_journals_1449369369
source Free Full-Text Journals in Chemistry
title Acid Phosphatases from the Liver of Labeo rohita
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-26T02%3A29%3A32IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Acid%20Phosphatases%20from%20the%20Liver%20of%20Labeo%20rohita&rft.jtitle=Biological%20&%20pharmaceutical%20bulletin&rft.au=Siddiqua,%20Aisha&rft.date=2008-05-01&rft.volume=31&rft.issue=5&rft.spage=802&rft.pages=802-&rft.issn=0918-6158&rft.eissn=1347-5215&rft_id=info:doi/&rft_dat=%3Cproquest%3E3121406941%3C/proquest%3E%3Cgrp_id%3Ecdi_FETCH-proquest_journals_14493693693%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1449369369&rft_id=info:pmid/&rfr_iscdi=true