Purification and characterization of a trypsin-like enzyme from the hepatopancreas of crayfish (Procambarus clarkii)

N. Guizani, M. R. Marshall, C. I. Wei

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

1. 1. A trypsin-like enzyme was purified from the hepatopancreas of Louisiana swamp crayfish, Procambarus clarkii, by a combination of hydrophobic interaction chromatography, molecular sieving and ion-exchange chromatography. 2. 2. The enzyme had a molecular weight of 33.6 kDa on SDS-PAGE and an isoelectric point of 3.0. 3. 3. The enzyme exhibited optimal activity at pH 8.0 and an optimal temperature of 55°C. It was stable in the pH range of 7.5-9.0, but unstable above 55°C. 4. 4. The tryptic activity was inhibited by phenylmethyl sulfonyl fluoride and other well-established trypsin inhibitors. 5. 5. Immunological study showed that crayfish trypsin-like enzyme shared structural components with bovine trypsin.

Original languageEnglish
Pages (from-to)809-815
Number of pages7
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume103
Issue number4
DOIs
Publication statusPublished - 1992

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Hepatopancreas
Astacoidea
Trypsin
Purification
Enzymes
Chromatography
Trypsin Inhibitors
Wetlands
Ion Exchange Chromatography
Isoelectric Point
Hydrophobic and Hydrophilic Interactions
Polyacrylamide Gel Electrophoresis
Ion exchange
Molecular Weight
Molecular weight
Temperature

ASJC Scopus subject areas

  • Biochemistry
  • Physiology

Cite this

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abstract = "1. 1. A trypsin-like enzyme was purified from the hepatopancreas of Louisiana swamp crayfish, Procambarus clarkii, by a combination of hydrophobic interaction chromatography, molecular sieving and ion-exchange chromatography. 2. 2. The enzyme had a molecular weight of 33.6 kDa on SDS-PAGE and an isoelectric point of 3.0. 3. 3. The enzyme exhibited optimal activity at pH 8.0 and an optimal temperature of 55°C. It was stable in the pH range of 7.5-9.0, but unstable above 55°C. 4. 4. The tryptic activity was inhibited by phenylmethyl sulfonyl fluoride and other well-established trypsin inhibitors. 5. 5. Immunological study showed that crayfish trypsin-like enzyme shared structural components with bovine trypsin.",
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AU - Wei, C. I.

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N2 - 1. 1. A trypsin-like enzyme was purified from the hepatopancreas of Louisiana swamp crayfish, Procambarus clarkii, by a combination of hydrophobic interaction chromatography, molecular sieving and ion-exchange chromatography. 2. 2. The enzyme had a molecular weight of 33.6 kDa on SDS-PAGE and an isoelectric point of 3.0. 3. 3. The enzyme exhibited optimal activity at pH 8.0 and an optimal temperature of 55°C. It was stable in the pH range of 7.5-9.0, but unstable above 55°C. 4. 4. The tryptic activity was inhibited by phenylmethyl sulfonyl fluoride and other well-established trypsin inhibitors. 5. 5. Immunological study showed that crayfish trypsin-like enzyme shared structural components with bovine trypsin.

AB - 1. 1. A trypsin-like enzyme was purified from the hepatopancreas of Louisiana swamp crayfish, Procambarus clarkii, by a combination of hydrophobic interaction chromatography, molecular sieving and ion-exchange chromatography. 2. 2. The enzyme had a molecular weight of 33.6 kDa on SDS-PAGE and an isoelectric point of 3.0. 3. 3. The enzyme exhibited optimal activity at pH 8.0 and an optimal temperature of 55°C. It was stable in the pH range of 7.5-9.0, but unstable above 55°C. 4. 4. The tryptic activity was inhibited by phenylmethyl sulfonyl fluoride and other well-established trypsin inhibitors. 5. 5. Immunological study showed that crayfish trypsin-like enzyme shared structural components with bovine trypsin.

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