Bence Jones proteins and light chains of immunoglobulins. XIII. Effect of elastase like and chymotrypsin like neutral proteases derived from human granulocytes on Bence Jones proteins

Alan Solomon, W. Schmidt, K. Havemann

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Abstract

Bence Jones proteins can be cleaved specifically by several types of endopeptidases into fragments corresponding to the amino terminal, variant (V(L)) portion and to the carboxyl terminal, constant (C(L)) portion of the light polypeptide chain. Two types of neutral proteases, designated elastase like (ELP) and chymotrypsin like (CLP), have been isolated and purified from human polymorphonuclear leukocytes. Because these proteases have defined proteolytic activity under physiologic conditions for several types of human proteins, the authors have investigated their effect on human Bence Jones proteins. Incubation of kappa type or λ type Bence Jones proteins with ELP or CLP under appropriate conditions resulted in cleavage of both types of light chains as evident by immunochemical and electrophoretic analyses. Treatment with ELP or CLP of one kappa Bence Jones protein resulted in the formation of a single component that had antigenic and electrophoretic properties similar to the V(L) fragment derived from pepsin digestion of the native protein. No component corresponding to the C(L) could be detected immunochemically or electrophoretically. Studies of isolated pepsin labile (37°C) and pepsin stable (55°C) C(L) fragments demonstrated the marked susceptibility of the carboxyl terminal half of the light chain to proteolysis by the leukocyte derived neutral proteases. Incubation with ELP of three other kappa Bence Jones proteins and three reduced alkylated λ Bence Jones proteins resulted, in each case, in the formation of a homogeneous component which was electrophoretically and immunochemically distinct from the pepsin derived V(L) fragment. An identical component could also be formed by incubating a pepsin derived V(L) fragment with ELP. In the ELP treated samples, no C(L) related material was detected electrophoretically or immunochemically with antisera possessing specificity for C(L) antigenic determinants present on the unfolded light polypeptide chain or on the isolated C(L). The component formed by ELP or CLP treatment of certain Bence Jones proteins thus appears to be V(L) related, but lacks the idiotypic antigenic determinant present on the native protein. In this respect, these neutral protease derived light chain components are similar to the amyloid like V(L) fragments generated in vitro from certain endopeptidase treated Bence Jones proteins.

Original languageEnglish (US)
Pages (from-to)1010-1014
Number of pages5
JournalJournal of Immunology
Volume117
Issue number3
StatePublished - Dec 1 1976

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Bence Jones Protein
Chymases
Immunoglobulin Light Chains
Pancreatic Elastase
Granulocytes
Pepsin A
Light
Peptide Hydrolases
Endopeptidases
Proteolysis
Epitopes
Peptides
Chymotrypsin
Amyloid
Immune Sera
Proteins
Neutrophils
Leukocytes

All Science Journal Classification (ASJC) codes

  • Immunology

Cite this

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title = "Bence Jones proteins and light chains of immunoglobulins. XIII. Effect of elastase like and chymotrypsin like neutral proteases derived from human granulocytes on Bence Jones proteins",
abstract = "Bence Jones proteins can be cleaved specifically by several types of endopeptidases into fragments corresponding to the amino terminal, variant (V(L)) portion and to the carboxyl terminal, constant (C(L)) portion of the light polypeptide chain. Two types of neutral proteases, designated elastase like (ELP) and chymotrypsin like (CLP), have been isolated and purified from human polymorphonuclear leukocytes. Because these proteases have defined proteolytic activity under physiologic conditions for several types of human proteins, the authors have investigated their effect on human Bence Jones proteins. Incubation of kappa type or λ type Bence Jones proteins with ELP or CLP under appropriate conditions resulted in cleavage of both types of light chains as evident by immunochemical and electrophoretic analyses. Treatment with ELP or CLP of one kappa Bence Jones protein resulted in the formation of a single component that had antigenic and electrophoretic properties similar to the V(L) fragment derived from pepsin digestion of the native protein. No component corresponding to the C(L) could be detected immunochemically or electrophoretically. Studies of isolated pepsin labile (37°C) and pepsin stable (55°C) C(L) fragments demonstrated the marked susceptibility of the carboxyl terminal half of the light chain to proteolysis by the leukocyte derived neutral proteases. Incubation with ELP of three other kappa Bence Jones proteins and three reduced alkylated λ Bence Jones proteins resulted, in each case, in the formation of a homogeneous component which was electrophoretically and immunochemically distinct from the pepsin derived V(L) fragment. An identical component could also be formed by incubating a pepsin derived V(L) fragment with ELP. In the ELP treated samples, no C(L) related material was detected electrophoretically or immunochemically with antisera possessing specificity for C(L) antigenic determinants present on the unfolded light polypeptide chain or on the isolated C(L). The component formed by ELP or CLP treatment of certain Bence Jones proteins thus appears to be V(L) related, but lacks the idiotypic antigenic determinant present on the native protein. In this respect, these neutral protease derived light chain components are similar to the amyloid like V(L) fragments generated in vitro from certain endopeptidase treated Bence Jones proteins.",
author = "Alan Solomon and W. Schmidt and K. Havemann",
year = "1976",
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T1 - Bence Jones proteins and light chains of immunoglobulins. XIII. Effect of elastase like and chymotrypsin like neutral proteases derived from human granulocytes on Bence Jones proteins

AU - Solomon, Alan

AU - Schmidt, W.

AU - Havemann, K.

PY - 1976/12/1

Y1 - 1976/12/1

N2 - Bence Jones proteins can be cleaved specifically by several types of endopeptidases into fragments corresponding to the amino terminal, variant (V(L)) portion and to the carboxyl terminal, constant (C(L)) portion of the light polypeptide chain. Two types of neutral proteases, designated elastase like (ELP) and chymotrypsin like (CLP), have been isolated and purified from human polymorphonuclear leukocytes. Because these proteases have defined proteolytic activity under physiologic conditions for several types of human proteins, the authors have investigated their effect on human Bence Jones proteins. Incubation of kappa type or λ type Bence Jones proteins with ELP or CLP under appropriate conditions resulted in cleavage of both types of light chains as evident by immunochemical and electrophoretic analyses. Treatment with ELP or CLP of one kappa Bence Jones protein resulted in the formation of a single component that had antigenic and electrophoretic properties similar to the V(L) fragment derived from pepsin digestion of the native protein. No component corresponding to the C(L) could be detected immunochemically or electrophoretically. Studies of isolated pepsin labile (37°C) and pepsin stable (55°C) C(L) fragments demonstrated the marked susceptibility of the carboxyl terminal half of the light chain to proteolysis by the leukocyte derived neutral proteases. Incubation with ELP of three other kappa Bence Jones proteins and three reduced alkylated λ Bence Jones proteins resulted, in each case, in the formation of a homogeneous component which was electrophoretically and immunochemically distinct from the pepsin derived V(L) fragment. An identical component could also be formed by incubating a pepsin derived V(L) fragment with ELP. In the ELP treated samples, no C(L) related material was detected electrophoretically or immunochemically with antisera possessing specificity for C(L) antigenic determinants present on the unfolded light polypeptide chain or on the isolated C(L). The component formed by ELP or CLP treatment of certain Bence Jones proteins thus appears to be V(L) related, but lacks the idiotypic antigenic determinant present on the native protein. In this respect, these neutral protease derived light chain components are similar to the amyloid like V(L) fragments generated in vitro from certain endopeptidase treated Bence Jones proteins.

AB - Bence Jones proteins can be cleaved specifically by several types of endopeptidases into fragments corresponding to the amino terminal, variant (V(L)) portion and to the carboxyl terminal, constant (C(L)) portion of the light polypeptide chain. Two types of neutral proteases, designated elastase like (ELP) and chymotrypsin like (CLP), have been isolated and purified from human polymorphonuclear leukocytes. Because these proteases have defined proteolytic activity under physiologic conditions for several types of human proteins, the authors have investigated their effect on human Bence Jones proteins. Incubation of kappa type or λ type Bence Jones proteins with ELP or CLP under appropriate conditions resulted in cleavage of both types of light chains as evident by immunochemical and electrophoretic analyses. Treatment with ELP or CLP of one kappa Bence Jones protein resulted in the formation of a single component that had antigenic and electrophoretic properties similar to the V(L) fragment derived from pepsin digestion of the native protein. No component corresponding to the C(L) could be detected immunochemically or electrophoretically. Studies of isolated pepsin labile (37°C) and pepsin stable (55°C) C(L) fragments demonstrated the marked susceptibility of the carboxyl terminal half of the light chain to proteolysis by the leukocyte derived neutral proteases. Incubation with ELP of three other kappa Bence Jones proteins and three reduced alkylated λ Bence Jones proteins resulted, in each case, in the formation of a homogeneous component which was electrophoretically and immunochemically distinct from the pepsin derived V(L) fragment. An identical component could also be formed by incubating a pepsin derived V(L) fragment with ELP. In the ELP treated samples, no C(L) related material was detected electrophoretically or immunochemically with antisera possessing specificity for C(L) antigenic determinants present on the unfolded light polypeptide chain or on the isolated C(L). The component formed by ELP or CLP treatment of certain Bence Jones proteins thus appears to be V(L) related, but lacks the idiotypic antigenic determinant present on the native protein. In this respect, these neutral protease derived light chain components are similar to the amyloid like V(L) fragments generated in vitro from certain endopeptidase treated Bence Jones proteins.

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