Separation of the Human Leucocy te Enzymes. Alanine Aminopeptidase, Cathepsin G, Collagenase, Elastase and Myeloperoxidase

Engelbrecht, Siegfried; Pieper, Edith; Macartney, Henry W.; Rautenberg, Wilfried; Wenzel, Herbert R.; Tschesche, Harald

doi:10.1515/bchm2.1982.363.1.305

Cited by 40 publications

(12 citation statements)

References 10 publications

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“…Leucocytes were isolated from buffy coat according to the method described in [14]. PMN leucocyte collagenase was purified to homogeneity as recently published [15].…”

Section: Purification Of Pain Leucocyte Collagenase Activation and Ementioning

confidence: 99%

Inactivation of human plasma α₁‐proteinase inhibitor by human PMN leucocyte collagenase

1990

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Highly purified human polymorphonuclear leucocyte collagenase cleaved human e-l-proteinase inhibitor (~I-PI) at the carboxyl site of Phe asz (PT). The inhibitor was thereby rapidly inactivated and generated a primary degradation product as shown by reverse-phase HPLC and N-terminal sequencing. Prolonged incubation of the modified inhibitor with polymorphonuclear leucocyte collagenase led to the generation of a secondary degradation product with additional cleavage at the carboxyl site of Pro 3s7 (Pz).

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“…Leucocytes were isolated from buffy coat according to the method described in [14]. PMN leucocyte collagenase was purified to homogeneity as recently published [15].…”

Section: Purification Of Pain Leucocyte Collagenase Activation and Ementioning

confidence: 99%

Inactivation of human plasma α₁‐proteinase inhibitor by human PMN leucocyte collagenase

1990

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“…Latent human polymorphonuclear leukocyte collagenase and gelatinase were prepared from buffy coat s described elsewhere (2,4,20). The active enzymes were prepared by activating the latent enzymes with either trypsin or mercurial compounds (4,20).…”

Section: Preparation Of Leukocyte Collagenase and Gelatinase Standardsmentioning

confidence: 99%

Enzyme Linked Immunosorbent Assays (ELISA) for the Quantitative Determination of Human Leukocyte Collagenase and Gelatinase

Bergmann¹,

Michaelis²,

Oberhoff³

et al. 1989

Clinical Chemistry and Laboratory Medicine

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Summary:A competitive and a sandwich enzyme linked immunosorbent assay (ELISA) were developed for human leukocyte collagenase and gelatinase.The competitive assay could detect 0.5 ng collagenase and 0.05 ng gelatinase. The detection limit of the sandwich ELISA was 0.05 ng for collagenase and 0.02 ng for gelatinase.No cross reactivity between human leukocyte collagenase and gelatinase was detected. The sandwich ELISA was used to determine plasma levels of these enzymes. The 90% ränge for collagenase was between 0 and 50 g/l; the 90% ränge for gelatinase was between 27 and 94 g/l.

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“…Cathepsin G (EC 3.4.21.20) was purified from buffy coats of healthy blood donors according to the method of Engelbrecht et al (1982). Trypsin (bovine pancreas) was purchased from Serva (Heidelberg, Germany) and elastase (EC 3.4.21.37) from Elastin Products (Owensville, MO, U.S.A.).…”

Section: Materials and Methods Enzymesmentioning

confidence: 99%

Purification of a serine-proteinase inhibitor from human articular cartilage. Identity with the acid-stable proteinase inhibitor of mucous secretions

Böhm

Deutzmann

Burkhardt

1991

Biochemical Journal

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An inhibitor of the serine proteinases human leucocyte elastase (EC 3.4.21.37), of cathepsin G (EC 3.4.21.20) and of trypsin (EC 3.4.21.4) has been purified from human articular cartilage. The apparent Mr of the cationic (pI greater than 10) protein was determined to 15,000 by SDS/PAGE. It was shown to cross-react in Western blot with a specific antibody to a recombinant-derived serine-proteinase inhibitor of human mucous secretions. Identity of both inhibitors is indicated by the determination of the N-terminal amino acid sequence of the cartilage-derived serine-proteinase inhibitor. In all 24 residues the cartilage inhibitor was shown to be identical with the human secretory leucocyte proteinase inhibitor (‘SLPI’). The inhibitor molecule may play a crucial role in the protection of cartilage matrix proteins against proteolytic attack.

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Separation of the Human Leucocy te Enzymes. Alanine Aminopeptidase, Cathepsin G, Collagenase, Elastase and Myeloperoxidase

Cited by 40 publications

References 10 publications

Inactivation of human plasma α₁‐proteinase inhibitor by human PMN leucocyte collagenase

Inactivation of human plasma α₁‐proteinase inhibitor by human PMN leucocyte collagenase

Enzyme Linked Immunosorbent Assays (ELISA) for the Quantitative Determination of Human Leukocyte Collagenase and Gelatinase

Purification of a serine-proteinase inhibitor from human articular cartilage. Identity with the acid-stable proteinase inhibitor of mucous secretions

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Separation of the Human Leucocy te Enzymes. Alanine Aminopeptidase, Cathepsin G, Collagenase, Elastase and Myeloperoxidase

Cited by 40 publications

References 10 publications

Inactivation of human plasma α1‐proteinase inhibitor by human PMN leucocyte collagenase

Inactivation of human plasma α1‐proteinase inhibitor by human PMN leucocyte collagenase

Enzyme Linked Immunosorbent Assays (ELISA) for the Quantitative Determination of Human Leukocyte Collagenase and Gelatinase

Purification of a serine-proteinase inhibitor from human articular cartilage. Identity with the acid-stable proteinase inhibitor of mucous secretions

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Inactivation of human plasma α₁‐proteinase inhibitor by human PMN leucocyte collagenase

Inactivation of human plasma α₁‐proteinase inhibitor by human PMN leucocyte collagenase