Modification of beta-2-microglobulin in sera from patients with small cell lung cancer: evidence for involvement of a serine protease.
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Modification of beta-2-microglobulin in sera from patients with small cell lung cancer: evidence for involvement of a serine protease. / Nissen, Mogens Holst; Bjerrum, Ole Jannik; Plesner, T; Wilken, M; Rørth, M.
In: Clinical and Experimental Immunology, Vol. 67, No. 2, 1987, p. 425-32.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Modification of beta-2-microglobulin in sera from patients with small cell lung cancer: evidence for involvement of a serine protease.
AU - Nissen, Mogens Holst
AU - Bjerrum, Ole Jannik
AU - Plesner, T
AU - Wilken, M
AU - Rørth, M
N1 - Keywords: Carcinoma, Small Cell; Endopeptidases; Humans; Hydrogen-Ion Concentration; Immunoelectrophoresis, Two-Dimensional; Lung Neoplasms; Protease Inhibitors; Serine Endopeptidases; Temperature; beta 2-Microglobulin
PY - 1987
Y1 - 1987
N2 - Modification of beta-2-microglobulin has been shown to occur in vitro in serum of patients suffering of small cell lung cancer, where it clearly correlated to the clinical course of disease. The cause of serum beta-2-microglobulin modification occurring in these patients is investigated in the present study. This revealed that modification of beta-2-microglobulin is due to cleavage by a serine protease, which is dependent on divalent cations and has a trypsin-like specificity. The process showed the following characteristics: pH optimum at 8.5, heat inactivation by incubation at 56 degrees C for 20 min and temperature optimum at 20 degrees C.
AB - Modification of beta-2-microglobulin has been shown to occur in vitro in serum of patients suffering of small cell lung cancer, where it clearly correlated to the clinical course of disease. The cause of serum beta-2-microglobulin modification occurring in these patients is investigated in the present study. This revealed that modification of beta-2-microglobulin is due to cleavage by a serine protease, which is dependent on divalent cations and has a trypsin-like specificity. The process showed the following characteristics: pH optimum at 8.5, heat inactivation by incubation at 56 degrees C for 20 min and temperature optimum at 20 degrees C.
M3 - Journal article
C2 - 3038438
VL - 67
SP - 425
EP - 432
JO - Clinical and Experimental Immunology, Supplement
JF - Clinical and Experimental Immunology, Supplement
SN - 0964-2536
IS - 2
ER -
ID: 8746804