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Neuraminidase and Hematopoietic Factors from Human Urine

Human urinary neuraminidase, an enzyme that releases sialic acid from hematopoietic factors found in urinary preparations, was partially characterized, and a method was developed to derive these hematopoietic factors free of enzyme activity. Neuraminidase in urinary preparations from healthy humans... Full description

Journal Title: Pathobiology 1986, Vol.54(4), pp.225-233
Main Author: Shimizu, Tomoe
Other Authors: Noguchi, Junko , Schuebel, Kornel , Miyake, Takaji , Murphy, Jr, Martin J
Format: Electronic Article Electronic Article
Language: English
Subjects:
Quelle: Karger Journals (S. Karger AG)
ID: ISSN: 1015-2008 ; E-ISSN: 1423-0291 ; DOI: 10.1159/000163359
Link: https://www.karger.com/Article/FullText/163359
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recordid: karger_s163359
title: Neuraminidase and Hematopoietic Factors from Human Urine
format: Article
creator:
  • Shimizu, Tomoe
  • Noguchi, Junko
  • Schuebel, Kornel
  • Miyake, Takaji
  • Murphy, Jr, Martin J
subjects:
  • Paper
  • Erythropoietin
  • Thrombopoietin
  • Neuraminidase
  • Aplastic Anemia
  • Colony Stimulating Factor
  • Medicine
  • Biology
ispartof: Pathobiology, 1986, Vol.54(4), pp.225-233
description: Human urinary neuraminidase, an enzyme that releases sialic acid from hematopoietic factors found in urinary preparations, was partially characterized, and a method was developed to derive these hematopoietic factors free of enzyme activity. Neuraminidase in urinary preparations from healthy humans and aplastic anemic (AA) patients had optimal activity at pH 5.3 and hydrolyzed both α2 → 3 and α2 → 6 type ketosidic linkages of N-acetyl-neuramin lactose and α1-acid glycoprotein. When subjected to Sephacryl S-300 gel filtration, urinary neuraminidase showed a single peak of activity with an apparent molecular weight of 380,000 daltons, even under denaturing conditions (6 M guanidine hydrochloride). Furthermore, among a variety of compounds tested, no potent inhibitor of the enzyme was found. Heat treatment of AA urinary preparations eliminated about 80% of neuraminidase activity, while successive two-step ethanol precipitation eliminated residual enzyme. Erythropoietin, megakaryocyte colony-stimulating factor (CSF) and granulocyte/macrophage CSF activities were retained after these treatments.
language: eng
source: Karger Journals (S. Karger AG)
identifier: ISSN: 1015-2008 ; E-ISSN: 1423-0291 ; DOI: 10.1159/000163359
fulltext: fulltext
issn:
  • 1015-2008
  • 10152008
  • 1423-0291
  • 14230291
url: Link


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subjectPaper ; Erythropoietin ; Thrombopoietin ; Neuraminidase ; Aplastic Anemia ; Colony Stimulating Factor ; Medicine ; Biology
descriptionHuman urinary neuraminidase, an enzyme that releases sialic acid from hematopoietic factors found in urinary preparations, was partially characterized, and a method was developed to derive these hematopoietic factors free of enzyme activity. Neuraminidase in urinary preparations from healthy humans and aplastic anemic (AA) patients had optimal activity at pH 5.3 and hydrolyzed both α2 → 3 and α2 → 6 type ketosidic linkages of N-acetyl-neuramin lactose and α1-acid glycoprotein. When subjected to Sephacryl S-300 gel filtration, urinary neuraminidase showed a single peak of activity with an apparent molecular weight of 380,000 daltons, even under denaturing conditions (6 M guanidine hydrochloride). Furthermore, among a variety of compounds tested, no potent inhibitor of the enzyme was found. Heat treatment of AA urinary preparations eliminated about 80% of neuraminidase activity, while successive two-step ethanol precipitation eliminated residual enzyme. Erythropoietin, megakaryocyte colony-stimulating factor (CSF) and granulocyte/macrophage CSF activities were retained after these treatments.
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Human urinary neuraminidase, an enzyme that releases sialic acid from hematopoietic factors found in urinary preparations, was partially characterized, and a method was developed to derive these hematopoietic factors free of enzyme activity. Neuraminidase in urinary preparations from healthy humans and aplastic anemic (AA) patients had optimal activity at pH 5.3 and hydrolyzed both α2 → 3 and α2 → 6 type ketosidic linkages of N-acetyl-neuramin lactose and α1-acid glycoprotein. When subjected to Sephacryl S-300 gel filtration, urinary neuraminidase showed a single peak of activity with an apparent molecular weight of 380,000 daltons, even under denaturing conditions (6 M guanidine hydrochloride). Furthermore, among a variety of compounds tested, no potent inhibitor of the enzyme was found. Heat treatment of AA urinary preparations eliminated about 80% of neuraminidase activity, while successive two-step ethanol precipitation eliminated residual enzyme. Erythropoietin, megakaryocyte colony-stimulating factor (CSF) and granulocyte/macrophage CSF activities were retained after these treatments.

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Human urinary neuraminidase, an enzyme that releases sialic acid from hematopoietic factors found in urinary preparations, was partially characterized, and a method was developed to derive these hematopoietic factors free of enzyme activity. Neuraminidase in urinary preparations from healthy humans and aplastic anemic (AA) patients had optimal activity at pH 5.3 and hydrolyzed both α2 → 3 and α2 → 6 type ketosidic linkages of N-acetyl-neuramin lactose and α1-acid glycoprotein. When subjected to Sephacryl S-300 gel filtration, urinary neuraminidase showed a single peak of activity with an apparent molecular weight of 380,000 daltons, even under denaturing conditions (6 M guanidine hydrochloride). Furthermore, among a variety of compounds tested, no potent inhibitor of the enzyme was found. Heat treatment of AA urinary preparations eliminated about 80% of neuraminidase activity, while successive two-step ethanol precipitation eliminated residual enzyme. Erythropoietin, megakaryocyte colony-stimulating factor (CSF) and granulocyte/macrophage CSF activities were retained after these treatments.

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