Purification and physicochemical characterization of a new rat plasma proteinase inhibitor, α1-inhibitor III

Esnard, F.; Gauthier, Francis

doi:10.1016/0005-2744(80)90244-2

Cited by 42 publications

(25 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Dotted lines indicate absorbancy at 280 nm. TABLE 2. a-1-Antitrypsin and a-macroglobulin activities o f several mammalian sera a-1-Antitrypsin and a-Macroglobulin in Mammals the latter seems to be a-l-inhibitor III, molecular weight of which was reported to be 215,000 (Esnard and Gauthier 1980). Under the assay conditions used, the sera of the other species contained no trypsin inhibitor of which the molecular weight is in the neighborhood of 200,000.…”

Section: Resultsmentioning

confidence: 91%

Comparative studies on the serum levels of .ALPHA.-1-antitrypsin and .ALPHA.-macroglobulin in several mammals.

Takahara

Nakamura

Yamamoto

et al. 1983

Tohoku J. Exp. Med.

View full text Add to dashboard Cite

The sera of human, cattle, horse, sheep, goat, pig, dog, rabbit, guinea pig, rat, hamster, and mouse were assayed for total trypsin-inhibiting capacity, and for concentrations of a-l-antitrypsin and a-macroglobulin. The rodents examined showed striking species differences: the a-l-antitrypsin levels of mouse, rat, and guinea pig were more than twice the human level, while the a-macroglobulin levels of hamster and guinea pig were 340 and 40%, respectively, of the human level. On the other hand, little variations were found among the large domestic animals, their levels of the two inhibitors being similar to those of the human. --serum trypsininhibiting capacity; a-l-antitrypsin; a-macroglobulin

show abstract

Section: Resultsmentioning

confidence: 91%

Comparative studies on the serum levels of .ALPHA.-1-antitrypsin and .ALPHA.-macroglobulin in several mammals.

Takahara

Nakamura

Yamamoto

et al. 1983

Tohoku J. Exp. Med.

View full text Add to dashboard Cite

show abstract

“…Two of these inhibitors, cal-PI and RPI I, have properties suggesting them to be identical with the R1 and R2 components previously isolated from rat serum (Rosenberg et al, 1976 (Ganrot, 1973) or to czl-inhibitor III (Esnard & Gauthier, 1980) whose M, values are greater than 200000. Further, antithrombin III was removed during the first purification step of RPI II.…”

Section: Discussionmentioning

confidence: 51%

Proteinase inhibitors in rat serum. Purification and partial characterization of three functionally distinct trypsin inhibitors

Kuehn¹,

Rutschmann²,

Dahlmann³

et al. 1984

Biochemical Journal

View full text Add to dashboard Cite

Three different serine proteinase inhibitors were isolated from rat serum and purified to apparent homogeneity. One of the inhibitors appears to be homologous to a1-proteinase inhibitor isolated from man and other species, but the other two, designated rat proteinase inhibitor I and rat proteinase inhibitor II, seem to have no human counterpart. ac-Proteinase inhibitor (Mr 55000) inhibits trypsin, chymotrypsin and elastase, the three serine proteinases tested. Rat proteinase inhibitor I (M' 66000) is active towards trypsin and chymotrypsin, but is inactive towards elastase. Rat proteinase inhibitor II (M, 65000) is an effective inhibitor of trypsin only. Their contributions to the trypsin-inhibitory capacity of rat serum are about 68, 14 and 18% for a1-proteinase inhibitor, rat proteinase inhibitor I and rat proteinase inhibitor II respectively.

show abstract

“…However, the fact that the sedimentation rate seemed to increase stepwise with time of chase makes this possibility unlikely. The sedimentation rate of the ␣ form was similar to that of aldolase (data not shown), which has a sedimentation coefficient of 7.4 S (Stellwagen and Schachman, 1962); that of secreted ␣ 1 I 3 is 8.6 S (Esnard and Gauthier, 1980).…”

Section: Resultsmentioning

confidence: 65%

“…In this study we have analyzed the folding of ␣ 1 -inhibitor 3 (␣ 1 I 3 ), a 180 -200 kDa proteinase inhibitor secreted by rodent hepatocytes (Esnard and Gauthier, 1980;Geiger et al, 1987;Sjöberg et al, 1991). ␣ 1 I 3 shows sequence homology with ␣ 2 -macroglobulin and the complement components 3 and 4 (Braciak et al, 1988;Sottrup-Jensen, 1989).…”

mentioning

confidence: 99%

Posttranslational Folding of α1-Inhibitor 3

Wassler

Esnard

Fries

1995

Journal of Biological Chemistry

View full text Add to dashboard Cite

␣ 1 -Inhibitor 3 (␣ 1 I 3 ) is a rodent-specific proteinase inhibitor of about 190 kDa belonging to the ␣ 2 -macroglobulin family. It consists of five globular domains, three of which are connected by disulfide bridges, and contains an intramolecular thiol ester which can react with attacking proteinases. To explore the folding of newly synthesized ␣ 1 I 3 , we have used rat hepatocytes and pulsechase experiments. In one of the analyses, the radiolabeled protein was isolated from cell lysates by immunoprecipitation and its Asp-Pro bonds cleaved by treatment with formic acid. The size of the major fragment, as assessed by electrophoresis under nonreducing conditions, was found to increase from 100 to 150 kDa upon the chasing. This result, together with knowledge of the positions of the cleavage sites and the disulfide arrangement, indicates that one of the interdomain disulfide bonds is formed after the synthesis of the polypeptide. Analysis of the same material by limited proteolysis and by velocity centrifugation showed that the folded regions became larger and that the protein became more compact; the thiol ester was found to be formed after these conformational changes. These results suggest that the domains of ␣ 1 I 3 are only partially developed directly after the synthesis of the polypeptide and that they acquire their final structure as the protein condenses and the domains interact with one another.

show abstract

Purification and physicochemical characterization of a new rat plasma proteinase inhibitor, α1-inhibitor III

Cited by 42 publications

References 24 publications

Comparative studies on the serum levels of .ALPHA.-1-antitrypsin and .ALPHA.-macroglobulin in several mammals.

Comparative studies on the serum levels of .ALPHA.-1-antitrypsin and .ALPHA.-macroglobulin in several mammals.

Proteinase inhibitors in rat serum. Purification and partial characterization of three functionally distinct trypsin inhibitors

Posttranslational Folding of α1-Inhibitor 3

Contact Info

Product

Resources

About