Über Proteaseinhibitoren, IV. Isolierung von Protease-Inhibitoren mit Hilfe wasserunlöslicher Enzym-Harze

Fritz, Hans; Schult, H.; Hutzel, M.; Wiedemann, Michael; Werle, E.

doi:10.1515/bchm2.1967.348.1.308

Cited by 48 publications

(8 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The faint band after electrophoresis at pH 4-3 is probably a contami¬ nant but the heavy bands may both be caused by trypsin inhibitors of similar molecular weight since Fritz et al (1967) obtained the same results when purifying a trypsin inhibitor from the seminal vesicles of mice. The faint band after electrophoresis at pH 4-3 is probably a contami¬ nant but the heavy bands may both be caused by trypsin inhibitors of similar molecular weight since Fritz et al (1967) obtained the same results when purifying a trypsin inhibitor from the seminal vesicles of mice.…”

Section: Discussionmentioning

confidence: 74%

“…Acrosomal extracts of epididymal and capacitated spermatozoa have high acrosin activity whereas activity cannot be detected in acrosomal extracts of ejaculated sperma¬ tozoa until after chromatography of the extracts (Zaneveld et al, 1969). 388 L. J. D. Zaneveld et al Haendle, Fritz, Trautschold & Werle (1965) and Fritz, Schult, Hutzel, Wiedemann & Werle (1967) isolated a trypsin inhibitor from the seminal vesicles of mice using a resin to which trypsin was attached that specifically bound the inhibitor. 388 L. J. D. Zaneveld et al Haendle, Fritz, Trautschold & Werle (1965) and Fritz, Schult, Hutzel, Wiedemann & Werle (1967) isolated a trypsin inhibitor from the seminal vesicles of mice using a resin to which trypsin was attached that specifically bound the inhibitor.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Inhibition of Fertilization in Vivo by Pancreatic and Seminal Plasma Trypsin Inhibitors

Zaneveld¹,

Robertson²,

Kessler³

et al. 1971

Reproduction

134

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 74%

Section: Introductionmentioning

confidence: 99%

Inhibition of Fertilization in Vivo by Pancreatic and Seminal Plasma Trypsin Inhibitors

Zaneveld¹,

Robertson²,

Kessler³

et al. 1971

Reproduction

134

View full text Add to dashboard Cite

“…Insoluble trypsin polymer was made in this laboratory by coupling trypsin (Worthington 2X crystallized) to the copolymer of maleic anhydride and ethylene and crosslinking it with hexamethylenediamine (14,15). Insoluble polymer of swine pancreatic carboxypeptidase B was prepared by the same technique.…”

Section: Chiang Erdos Miwa Tague Coalsonmentioning

confidence: 99%

Isolation from a Salivary Gland of Granules Containing Renin and Kallikrein

Chiang

Erdös

Miwa

et al. 1968

Circulation Research

View full text Add to dashboard Cite

Granules of the submaxillary gland of the white mouse contain both kallikrein and renin. The granules were separated and concentrated in sequential centrifugation procedures. They were more stable at room temperature and in hypertonic sucrose solutions than in the cold or in isotonic solution. The amylase, acid phosphatase, renin, kallikrein, and benzoyl-L-arginine ethyl ester esterase contents of the granules were determined. Kallikrein and renin showed a similar distribution pattern after fractionation. Granular renin released the equivalent of 9. Electron micrographs of the isolated granules showed various forms; some were spherical and symmetrical, and others were amorphous. ADDITIONAL KEY WORDSsubmaxillary gland bradykinin angiotensin subcellular fractions electron microscopy differential centrifugation insoluble enzyme polymers kallidin• Granules originating from the rat submaxillary gland contain large amounts of kallikrein ( 1 ) . The appearance of these particles in electron micrographs is similar to that of pancreatic zymogen granules (2). Although the presence of renin in granules has been gaining acceptance, a definite relationship between granules and renin activity has not yet been established (3,4 ) . In addition to kallikrein, renin was found in the submaxillary glands of the white mouse (5-8). Renin activity is concentrated in the striated ducts which have granulated cells. These findings led us to study the subcellular distribution of renin and its relationship to kallikrein in the submaxillary gland of the white mouse. In the present communication we deal withFrom the Departments of Pharmacology and Pathology, University of Oklahoma, School of Medicine, Oklahoma City, Oklahoma 73104.This work was supported in part by U. S. Public Health Service Grant HE 08764 from the National Institutes of Health.When this work was done Dr. Miwa was a fellow of the Oklahoma Heart Association. His permanent address is Department of Medicine, Tohoku University, Sendai, Japan.Accepted for publication August 5, 1968.the isolation of an active, granular layer that contains both kallikrein and renin.Methods White male Swiss Webster mice (A. Sutter Co.) were killed by a sudden blow on the head without using anesthesia. The mice were over 90 days old and weighed about 50 g. Fresh, minced submaxillary glands were homogenized in batches of six pairs in a Dounce hand homogenizer. In the first series of experiments, the tissues were placed in a medium of 0.25M sucrose solution buffered with 0.005M Tris, pH 7.4, in an ice bath. A 10% (w/v) homogenate was prepared and filtered through four layers of gauze. The filtered homogenate was then fractionated using isotonic sucrose solutions and a refrigerated centrifuge as previously described (1).In the second series of experiments, all procedures were done at room temperature in a 0.88M sucrose solution buffered with 0.005M Tris, pH 7.4. The unbroken cells and tissues were removed by centrifugation at 120 g for 5 minutes using a Sorvall RC-2 centrifuge. The step was rep...

show abstract

“…There would seem to be compelling reasons for using affinity chromatography in the purification of inhibitors such as the one examined here. The procedure used-attachment of the inhibitor to an insolubilized enzyme followed by elution at low pH-has been used by a number of authors, for example Fritz et al (1967Fritz et al ( , 1969, Turkova et al (1973), andFeinstein et al (1974). In the present case the inhibitor prepared by affinity chroIllatography has been compared with the material isolated in more conventional ways.…”

Section: ·82mentioning

confidence: 99%

A Chymotrypsin Inhibitor From the Parasitic Nematode, Oesophagostomum radiatum

Willadsen¹

1977

Aust. Jnl. Of Bio. Sci.

View full text Add to dashboard Cite

An inhibitor of oc-chymotrypsin was isolated from O. radiatum by affinity chromatography, as well as by ion-exchange and molecular sieve chromatography. The inhibitor was associated with the cuticle or musculature of the parasite. It completely inhibited the esterolytic activity of chymotrypsin. Molecular sieve chromatography gave an apparent molecular weight of 9700 for the inhibitor alone and 32000 for the complex with chymotrypsin. This suggests reaction in a 1: 1 molar ratio. The inhibitor reacted with diisopropyl phosphoryl-chymotrypsin weakly, if at all.Measurement of the dissociation constants for the enzyme-inhibitor complexes gave values of 2·2 X 10-9 M for the product of affinity chromatography but less than 2 x 10-10 M for all other preparations. Possible explanations of this are discussed.

show abstract

Über Proteaseinhibitoren, IV. Isolierung von Protease-Inhibitoren mit Hilfe wasserunlöslicher Enzym-Harze

Cited by 48 publications

References 0 publications

Inhibition of Fertilization in Vivo by Pancreatic and Seminal Plasma Trypsin Inhibitors

Inhibition of Fertilization in Vivo by Pancreatic and Seminal Plasma Trypsin Inhibitors

Isolation from a Salivary Gland of Granules Containing Renin and Kallikrein

A Chymotrypsin Inhibitor From the Parasitic Nematode, Oesophagostomum radiatum

Contact Info

Product

Resources

About