Chemistry and Biochemistry of Proteinase Inhibitors From Mammalian Tissues

Fritz, Hans; Trautschold, I.; Haendle, H; Werle, E.

doi:10.1111/j.1749-6632.1968.tb20301.x

Cited by 36 publications

(14 citation statements)

References 11 publications

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“…Nielsen and Liener observed that endogenous proteases from Phaseolus vulgaris responded differently to a variety of inhibitors when either L-BAPA or azocasein or endogenous storage proteins were offered as substrate [20]. Generally, synthetic substrates yield higher inhibitory activities then natural proteins [21] Fritz et al [22] explain this phenomenon by suggesting that the larger, natural substrates are more difficult to displace from the active site to form the enzyme-inhibitor complex. If correct, this suggests that while the use of synthetic substrates is a more accurate means of determining the inhibitor content of materials [18], the use of natural substrates will yield a value that has more physiological relevance.…”

Section: Discussionmentioning

confidence: 94%

Quantitative Determination of Trypsin Inhibitory Activity in Complex Matrices

Spelbrink¹

2011

TOFSJ

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A quantitative assay using azocasein was developed to measure trypsin inhibitory activity in emulsions and other complex systems that are refractory to analysis. The method was tested for reproducibility on pure protein solutions as well as protein-containing material rich in fats and sugars, with special attention to emulsions. In the clean situation, the overall relative standard deviation was less than 6% while for the more complex systems it was less than 16%. The procedure proved robust against deliberate variations of temperature, incubation time and substrate concentration.

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Section: Discussionmentioning

confidence: 94%

Quantitative Determination of Trypsin Inhibitory Activity in Complex Matrices

Spelbrink¹

2011

TOFSJ

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“…In inhibitors with independent trypsin-and chymotrypsin-reactive sites, one may be modified but not the other (Belew and Eaker 1976). Alternatively, temporary inhibition may occur (Tschesche 1967;Fritz et al 1968;Tschesche and Klein 1968). In the present case, however, the change in the inhibitor is minimal and is seen as a decreased affinity for the enzyme which would not be detected in a normal assay.…”

Section: ·82mentioning

confidence: 45%

A Chymotrypsin Inhibitor From the Parasitic Nematode, Oesophagostomum radiatum

Willadsen¹

1977

Aust. Jnl. Of Bio. Sci.

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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.

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“…The method used for the separation of seminal plasma and spermatozoa produced preparations free from cytoplasmic-droplets, as had been reported by Dott & Dingle (1968 (Haendle et al, 1965;Fritz et al, 1968) (Fritz et al, 1968). The inhibitory effect of the preparation III cannot depend on the presence of salts, amino acids or other low molecular weight substances, because preparation III could be concentrated by membrane ultrafiltration without any distinct loss of inhibitor capacity.…”

Section: Discussionmentioning

confidence: 87%

“…Several investigations have since confirmed the presence in the semen of such inhibitory factor (s) against seminal fibrinolytic activity (von Kaulla & Shettles, 1953;Rasmussen & Albrechtsen, 1960;Di Bella, Panazzolo & Scarpa, 1966). Other proteolytic enzymes have also been shown to be sensitive to inhibitors present in ejaculated seminal fluid or in the secretions of male accessory sex glands (Haendle, Fritz, Trautschold & Werle, 1965;Fritz, Trautschold, Haendle & Werle, 1968). Moreover, the presence of a particular trypsin inhibitor could be demonstrated in bull, guinea-pig, hamster, mouse and rat seminal vesicle secretion as well as in the semen of man, boar and bull.…”

Section: Introductionmentioning

confidence: 99%