[56] Human α1-Antichymotrypsin

Travis, James; Morii, Mitsuyoshi

doi:10.1016/s0076-6879(81)80058-4

Cited by 25 publications

(14 citation statements)

References 6 publications

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“…DISCUSSION ␣ 1 -Antichymotrypsin was first isolated from human serum in 1965, but the purification procedure was lengthy and complicated (40). Since then, several groups have attempted to simplify the isolation procedure using a variety of chromatographic techniques (6,23,24,37,38,41,42). The yield and quality of ␣ 1 -antichymotrypsin was diverse, and two groups reported unexplained additional ␣ 1 -antichymotrypsin bands.…”

Section: Resultsmentioning

confidence: 99%

“…Isolation of ␣ 1 -Antichymotrypsin from Plasma-The preparation of human ␣ 1 -antichymotrypsin described here is a modification of the original method described by Travis et al (23,24) with all purification steps being performed at 4°C. Two hundred-ml samples of plasma from 30 healthy blood donors were each mixed with 200 ml of saturated ammonium sulfate for 30 min and then centrifuged at 1500 ϫ g for 30 min.…”

Section: Methodsmentioning

confidence: 99%

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Latent α1-Antichymotrypsin

Chang

Lomas

1998

Journal of Biological Chemistry

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␣ 1 -Antichymotrypsin is an acute phase protein that protects the tissues from damage by proteolytic enzymes, but previous studies have shown that ␣ 1 -antichymotrypsin within the lungs of patients with chronic bronchitis and emphysema is intact but inactive as an inhibitor. Ammonium sulfate fractionation followed by blue Sepharose and DNA-Sepharose chromatography was used to isolate small amounts of intact, monomeric but inactive ␣ 1 -antichymotrypsin from the plasma of 30 healthy blood donors. This species had a higher DNA binding affinity with more anodal electrophoretic mobility than native ␣ 1 -antichymotrypsin and was conformationally stable against thermal denaturation, 8 M urea, and 7 M guanidinium chloride. The protein was unable to accept synthetic reactive loop peptides, and the reactive loop was resistant to proteolytic cleavage at the P 5 -P 4 bond but could be cleaved between P 1 and P 3 . These data suggest that this new ␣ 1 -antichymotrypsin species was in a conformation similar to those of the crystallographically determined latent serpins, plasminogen activator inhibitor-1 and antithrombin. ␣ 1 -Antichymotrypsin from lung lavage migrated with the same electrophoretic mobility as the putative latent ␣ 1 -antichymotrypsin, suggesting that this is the inactive conformation described previously in the lungs of patients with chronic bronchitis and emphysema. This conformational transition of ␣ 1 -antichymotrypsin, from an active to an inactive state, within the lung may play an important role in the pathogenesis of chronic lung disease.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Latent α1-Antichymotrypsin

Chang

Lomas

1998

Journal of Biological Chemistry

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“…This indicates that the SCC antigen has the general property of serpins, such as ACT, which interacts with chymotrypsin to form an equimolar SDS-stable complex [17,18,231. It was reported that the complex of ACT with chymotrypsin dissociated spontaneously after 24 h and this slow dissociation resulted in the release of modified, inactive ACT, which was a slowly digested product, and of active chymotrypsin [23].…”

Section: Discussionmentioning

confidence: 99%

Serine protease inhibitor activity of recombinant squamous cell carcinoma antigen towards chymotrypsin, as demonstrated by sodium dodecyl sulfatepolyacrylamide gel electrophoresis

et al. 1995

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Squamous cell carcinoma (SCC) antigen was tested, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, for its ability to inhibit the activity of serine proteases, i.e., trypsin, chymotrypsin and elastase. We demonstrated that the serine protease inhibitor (serpin) of SCC antigen is specific for chymotrypsin. Preincubation of chymotrypsin with recombinant SCC antigen inhibited chymotryptic digestion of gelatin and ovalbumin through the formation of sodium dodecyl sulfate-stable complexes. These findings promote understanding of the biological functions of SCC antigen as serpin in the stratification of the normal squamous cells and in the malignant behavior of the tumor cells.

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“…Inhibitors were prepared as described: al-PI [6]; CT-Inh [7]; a,-AC by a slight modification of [8] as described in [9]. AT I11 was provided by the American Red Cross Blood Services Laboratory, a2-AP by Dr. D. Collen, University of Leuven, P aeruginosa protease and elastase by Dr. K. Morihara, Toho Pharmaceutical Co. (Kyoto, Japan), and human leucocyte elastase by Dr. Dave Johnson, East Tennessee State University.…”

Section: Methodsmentioning

confidence: 99%

Inactivation of human plasma serine proteinase inhibitors (serpins) by limited proteolysis of the reactive site loop with snake venom and bacterial metalloproteinases

Kress

1986

J of Cellular Biochemistry

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Human plasma serine proteinase inhibitors (serpins) gradually lost activity when incubated with catalytic amounts of snake venom or bacterial metalloproteinases. Electrophoretic analyses indicated that antithrombin III, C1-inhibitor, and alpha 2-antiplasmin had been converted by limited proteolysis into modified species which retained inhibitory activity. Further proteolytic attack resulted in the formation of inactivated inhibitors; alpha 1-proteinase inhibitor (alpha 1-antitrypsin) and alpha 1-antichymotrypsin were also enzymatically inactivated, but active intermediates were not detected. Sequence analyses indicated that the initial, noninactivating cleavage occurred in the amino-terminal region of the inhibitors. Inactivation resulted in all cases from the limited proteolysis of a single bond near, but not at, the reactive site bond in the carboxy-terminal region of the inhibitors. The results indicate that the serpins have two regions which are susceptible to limited proteolysis--one near the amino-terminal end and another in the exposed reactive site loop of the inhibitor.

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[56] Human α1-Antichymotrypsin

Cited by 25 publications

References 6 publications

Latent α1-Antichymotrypsin

Latent α1-Antichymotrypsin

Serine protease inhibitor activity of recombinant squamous cell carcinoma antigen towards chymotrypsin, as demonstrated by sodium dodecyl sulfatepolyacrylamide gel electrophoresis

Inactivation of human plasma serine proteinase inhibitors (serpins) by limited proteolysis of the reactive site loop with snake venom and bacterial metalloproteinases

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