Retinyl palmitate hydrolase activity in human liver

Retinyl palmitate hydrolase (RPH) activity was studied in human liver after the optimal conditions of the assay in normal human liver homogenates were determined. The mean activity was 118 ± 66 nmol · min−1 · g−1 (x̄ ± SD) protein in liver homogenates from six children and seven adults; no correlati...

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Veröffentlicht in:The American journal of clinical nutrition 1992-03, Vol.55 (3), p.729-733
Hauptverfasser: Mourey, MS, Amédée-Manesme, O
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description Retinyl palmitate hydrolase (RPH) activity was studied in human liver after the optimal conditions of the assay in normal human liver homogenates were determined. The mean activity was 118 ± 66 nmol · min−1 · g−1 (x̄ ± SD) protein in liver homogenates from six children and seven adults; no correlation was found between liver hydrolase activity and the enzyme endogenous substrate, ie, liver vitamin A concentrations. RPH activity was also studied in a human model of vitamin A deficiency represented by 22 children with biliary atresia: 11 patients with vitamin A deficiency (liver vitamin A concentration < 70 nmol/g wet wt of liver) and 11 patients with normal vitamin A status after vitamin A treatment. The enzymatic assay had to be conducted after the removal of endogenous bile salts by cholestyramine because bile salts are accumulated in the liver of children with biliary atresia. No correlation was found between RPH activity and vitamin A status.
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The mean activity was 118 ± 66 nmol · min−1 · g−1 (x̄ ± SD) protein in liver homogenates from six children and seven adults; no correlation was found between liver hydrolase activity and the enzyme endogenous substrate, ie, liver vitamin A concentrations. RPH activity was also studied in a human model of vitamin A deficiency represented by 22 children with biliary atresia: 11 patients with vitamin A deficiency (liver vitamin A concentration &lt; 70 nmol/g wet wt of liver) and 11 patients with normal vitamin A status after vitamin A treatment. The enzymatic assay had to be conducted after the removal of endogenous bile salts by cholestyramine because bile salts are accumulated in the liver of children with biliary atresia. 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Exocrine pancreas</subject><subject>Malformations</subject><subject>Medical sciences</subject><subject>regulation</subject><subject>retinyl palmitate hydrolase</subject><subject>vitamin A</subject><subject>Vitamin A - metabolism</subject><subject>Vitamin A Deficiency - enzymology</subject><issn>0002-9165</issn><issn>1938-3207</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1LxDAQhoMo67p69Cj0IN66O0mTpjnK4hcsCKLnkKZTNks_1qRd6L-3Sxc9eZqBeeZl5iHklsKSgkpWZmeblRDLZCmZOiNzqpIsThjIczIHABYrmopLchXCDoAynqUzMqNCAHA1J8kHdq4Zqmhvqtp1psNoOxS-rUzAyNjOHVw3RK6Jtn1tmqhyB_TX5KI0VcCbU12Qr-enz_VrvHl_eVs_bmLLgXdxIYpS2AQ4yNxwhhQFUM5ZRnOajn2aSWopSsUEplmhElOiwhRUDqzg4xsL8jDl7n373WPodO2CxaoyDbZ90JJlIpUyG8F4Aq1vQ_BY6r13tfGDpqCPkvRRkhZCJ-PSMfjuFNznNRZ_9GRlnN-f5iZYU5XeNNaFX0wwxpRKR0xOGI4SDg69DtZhY7FwHm2ni9b9c8AP_-KBUw</recordid><startdate>19920301</startdate><enddate>19920301</enddate><creator>Mourey, MS</creator><creator>Amédée-Manesme, O</creator><general>Elsevier Inc</general><general>American Society for Clinical Nutrition</general><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>7X8</scope></search><sort><creationdate>19920301</creationdate><title>Retinyl palmitate hydrolase activity in human liver</title><author>Mourey, MS ; Amédée-Manesme, O</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c404t-d5df5c30407ba42e1e50144281b16e506871c1e7925e68d93afe9e609b02d4193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Adolescent</topic><topic>Adult</topic><topic>Biliary atresia</topic><topic>Biliary Atresia - enzymology</topic><topic>Biological and medical sciences</topic><topic>Carboxylic Ester Hydrolases - metabolism</topic><topic>Child</topic><topic>Child, Preschool</topic><topic>cholestyramine</topic><topic>Cholic Acid</topic><topic>Cholic Acids - pharmacology</topic><topic>Gastroenterology. Liver. Pancreas. Abdomen</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Liver - enzymology</topic><topic>Liver. Biliary tract. Portal circulation. Exocrine pancreas</topic><topic>Malformations</topic><topic>Medical sciences</topic><topic>regulation</topic><topic>retinyl palmitate hydrolase</topic><topic>vitamin A</topic><topic>Vitamin A - metabolism</topic><topic>Vitamin A Deficiency - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mourey, MS</creatorcontrib><creatorcontrib>Amédée-Manesme, O</creatorcontrib><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>MEDLINE - Academic</collection><jtitle>The American journal of clinical nutrition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mourey, MS</au><au>Amédée-Manesme, O</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Retinyl palmitate hydrolase activity in human liver</atitle><jtitle>The American journal of clinical nutrition</jtitle><addtitle>Am J Clin Nutr</addtitle><date>1992-03-01</date><risdate>1992</risdate><volume>55</volume><issue>3</issue><spage>729</spage><epage>733</epage><pages>729-733</pages><issn>0002-9165</issn><eissn>1938-3207</eissn><coden>AJCNAC</coden><abstract>Retinyl palmitate hydrolase (RPH) activity was studied in human liver after the optimal conditions of the assay in normal human liver homogenates were determined. The mean activity was 118 ± 66 nmol · min−1 · g−1 (x̄ ± SD) protein in liver homogenates from six children and seven adults; no correlation was found between liver hydrolase activity and the enzyme endogenous substrate, ie, liver vitamin A concentrations. RPH activity was also studied in a human model of vitamin A deficiency represented by 22 children with biliary atresia: 11 patients with vitamin A deficiency (liver vitamin A concentration &lt; 70 nmol/g wet wt of liver) and 11 patients with normal vitamin A status after vitamin A treatment. The enzymatic assay had to be conducted after the removal of endogenous bile salts by cholestyramine because bile salts are accumulated in the liver of children with biliary atresia. No correlation was found between RPH activity and vitamin A status.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>1550049</pmid><doi>10.1093/ajcn/55.3.729</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record>
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subjects Adolescent
Adult
Biliary atresia
Biliary Atresia - enzymology
Biological and medical sciences
Carboxylic Ester Hydrolases - metabolism
Child
Child, Preschool
cholestyramine
Cholic Acid
Cholic Acids - pharmacology
Gastroenterology. Liver. Pancreas. Abdomen
Humans
Kinetics
Liver - enzymology
Liver. Biliary tract. Portal circulation. Exocrine pancreas
Malformations
Medical sciences
regulation
retinyl palmitate hydrolase
vitamin A
Vitamin A - metabolism
Vitamin A Deficiency - enzymology
title Retinyl palmitate hydrolase activity in human liver
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