N-acetyl- β-hexosaminidase activity in human breast milk

1. 1. The lysosomal enzyme, N-acetyl- β-hexosaminidase (HEX) is present in human breast milk. It is composed predominantly of “A” (heat-labile) and “B” (heat-stable) isozymes which coelute with the corresponding major serum isozymes on DE-52 ion-exchange chromatography. 2. 2. Total HEX activity in “...

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Veröffentlicht in:International journal of biochemistry 1982, Vol.14 (2), p.151-154
Hauptverfasser: Oberkotter, Linda V., Koldovsky, Otakar, Tenore, Alfred
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container_issue 2
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container_title International journal of biochemistry
container_volume 14
creator Oberkotter, Linda V.
Koldovsky, Otakar
Tenore, Alfred
description 1. 1. The lysosomal enzyme, N-acetyl- β-hexosaminidase (HEX) is present in human breast milk. It is composed predominantly of “A” (heat-labile) and “B” (heat-stable) isozymes which coelute with the corresponding major serum isozymes on DE-52 ion-exchange chromatography. 2. 2. Total HEX activity in “early” milk obtained at 2.8 ± 1.4 weeks post partum, is approx. 2.5-fold higher (87 ± 29 nmol/60'/mg protein, n = 10) than that of pregnancy serum (35.7 nmol/60'/mg protein) prior to delivery. 3. 3. These levels increase to greater than 3-fold (110 ± 20 nmol/60'/ mg protein, n = 13) as the milk matures (10.3 ± 4.2 weeks). 4. 4. The specific activity of HEX A in the milk changes little with time post partum, because absolute levels are decreasing simultaneous with decreases in milk protein. 5. 5. In contrast, HEX B specific activity is increased, as absolute levels (per volume) remain constant in the face of decreasing milk protein content. 6. 6. These changes result in a high degree of correlation ( r = 0.81) between time of lactation and % HEX A observed.
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The lysosomal enzyme, N-acetyl- β-hexosaminidase (HEX) is present in human breast milk. It is composed predominantly of “A” (heat-labile) and “B” (heat-stable) isozymes which coelute with the corresponding major serum isozymes on DE-52 ion-exchange chromatography. 2. 2. Total HEX activity in “early” milk obtained at 2.8 ± 1.4 weeks post partum, is approx. 2.5-fold higher (87 ± 29 nmol/60'/mg protein, n = 10) than that of pregnancy serum (35.7 nmol/60'/mg protein) prior to delivery. 3. 3. These levels increase to greater than 3-fold (110 ± 20 nmol/60'/ mg protein, n = 13) as the milk matures (10.3 ± 4.2 weeks). 4. 4. The specific activity of HEX A in the milk changes little with time post partum, because absolute levels are decreasing simultaneous with decreases in milk protein. 5. 5. In contrast, HEX B specific activity is increased, as absolute levels (per volume) remain constant in the face of decreasing milk protein content. 6. 6. 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The lysosomal enzyme, N-acetyl- β-hexosaminidase (HEX) is present in human breast milk. It is composed predominantly of “A” (heat-labile) and “B” (heat-stable) isozymes which coelute with the corresponding major serum isozymes on DE-52 ion-exchange chromatography. 2. 2. Total HEX activity in “early” milk obtained at 2.8 ± 1.4 weeks post partum, is approx. 2.5-fold higher (87 ± 29 nmol/60'/mg protein, n = 10) than that of pregnancy serum (35.7 nmol/60'/mg protein) prior to delivery. 3. 3. These levels increase to greater than 3-fold (110 ± 20 nmol/60'/ mg protein, n = 13) as the milk matures (10.3 ± 4.2 weeks). 4. 4. The specific activity of HEX A in the milk changes little with time post partum, because absolute levels are decreasing simultaneous with decreases in milk protein. 5. 5. In contrast, HEX B specific activity is increased, as absolute levels (per volume) remain constant in the face of decreasing milk protein content. 6. 6. These changes result in a high degree of correlation ( r = 0.81) between time of lactation and % HEX A observed.</description><subject>Adolescent</subject><subject>Adult</subject><subject>beta-N-Acetylhexosaminidases</subject><subject>Female</subject><subject>Hexosaminidase A</subject><subject>Hexosaminidase B</subject><subject>Hexosaminidases - blood</subject><subject>Hexosaminidases - metabolism</subject><subject>Humans</subject><subject>Isoenzymes - metabolism</subject><subject>Lactation</subject><subject>Milk Proteins - metabolism</subject><subject>Milk, Human - enzymology</subject><subject>Postpartum Period</subject><subject>Pregnancy</subject><subject>Time Factors</subject><issn>0020-711X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtOwzAQhr0AlVK4AUhZIVgEZpLYjjdIqOIlVbABiZ3lOhPVkEex04pei4NwJlJadclqpPkfo_kYO0G4REBxBZBALBHfzvPkQgFyHsMeG-7WB-wwhHcAVHmGAzYQmUAu5JCpp9hY6lZVHP18xzP6aoOpXeMKEygytnNL160i10SzRW2aaOrJhC6qXfVxxPZLUwU63s4Re727fRk_xJPn-8fxzSS2KZddbBIUWOZGoOVFkiUlFXlJMoVSKAkpcG5AFshVyrO0BIWZJZSFsr1FGiXSETvb9M59-7mg0OnaBUtVZRpqF0HLDFBiwntjtjFa34bgqdRz72rjVxpBrynpNQ69xqHzRP9R0tDHTrf9i2lNxS60RdTr1xud-ieXjrwO1lFjqXCebKeL1v1_4BegK3d8</recordid><startdate>1982</startdate><enddate>1982</enddate><creator>Oberkotter, Linda V.</creator><creator>Koldovsky, Otakar</creator><creator>Tenore, Alfred</creator><general>Elsevier B.V</general><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>1982</creationdate><title>N-acetyl- β-hexosaminidase activity in human breast milk</title><author>Oberkotter, Linda V. ; Koldovsky, Otakar ; Tenore, Alfred</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-a2161f8a61c5d242fed8fe730f69703055a07d1593543f0914ce17d9c7307a963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Adolescent</topic><topic>Adult</topic><topic>beta-N-Acetylhexosaminidases</topic><topic>Female</topic><topic>Hexosaminidase A</topic><topic>Hexosaminidase B</topic><topic>Hexosaminidases - blood</topic><topic>Hexosaminidases - metabolism</topic><topic>Humans</topic><topic>Isoenzymes - metabolism</topic><topic>Lactation</topic><topic>Milk Proteins - metabolism</topic><topic>Milk, Human - enzymology</topic><topic>Postpartum Period</topic><topic>Pregnancy</topic><topic>Time Factors</topic><toplevel>online_resources</toplevel><creatorcontrib>Oberkotter, Linda V.</creatorcontrib><creatorcontrib>Koldovsky, Otakar</creatorcontrib><creatorcontrib>Tenore, Alfred</creatorcontrib><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>International journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Oberkotter, Linda V.</au><au>Koldovsky, Otakar</au><au>Tenore, Alfred</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>N-acetyl- β-hexosaminidase activity in human breast milk</atitle><jtitle>International journal of biochemistry</jtitle><addtitle>Int J Biochem</addtitle><date>1982</date><risdate>1982</risdate><volume>14</volume><issue>2</issue><spage>151</spage><epage>154</epage><pages>151-154</pages><issn>0020-711X</issn><abstract>1. 1. The lysosomal enzyme, N-acetyl- β-hexosaminidase (HEX) is present in human breast milk. It is composed predominantly of “A” (heat-labile) and “B” (heat-stable) isozymes which coelute with the corresponding major serum isozymes on DE-52 ion-exchange chromatography. 2. 2. Total HEX activity in “early” milk obtained at 2.8 ± 1.4 weeks post partum, is approx. 2.5-fold higher (87 ± 29 nmol/60'/mg protein, n = 10) than that of pregnancy serum (35.7 nmol/60'/mg protein) prior to delivery. 3. 3. These levels increase to greater than 3-fold (110 ± 20 nmol/60'/ mg protein, n = 13) as the milk matures (10.3 ± 4.2 weeks). 4. 4. The specific activity of HEX A in the milk changes little with time post partum, because absolute levels are decreasing simultaneous with decreases in milk protein. 5. 5. In contrast, HEX B specific activity is increased, as absolute levels (per volume) remain constant in the face of decreasing milk protein content. 6. 6. These changes result in a high degree of correlation ( r = 0.81) between time of lactation and % HEX A observed.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>6461567</pmid><doi>10.1016/0020-711X(82)90155-0</doi><tpages>4</tpages></addata></record>
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subjects Adolescent
Adult
beta-N-Acetylhexosaminidases
Female
Hexosaminidase A
Hexosaminidase B
Hexosaminidases - blood
Hexosaminidases - metabolism
Humans
Isoenzymes - metabolism
Lactation
Milk Proteins - metabolism
Milk, Human - enzymology
Postpartum Period
Pregnancy
Time Factors
title N-acetyl- β-hexosaminidase activity in human breast milk
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