Über Proteaseinhibitoren, I. Isolierung und Charakterisierung des Trypsininhibitors aus Pankreasgewebe und Pankreassekret vom Hund

Fritz, Hans; Hartwich, G; Werle, E.

doi:10.1515/bchm2.1966.345.1.150

Cited by 81 publications

(23 citation statements)

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“…RD5, a diploid homozygous for the rad52-1 (33) allele was constructed from haploid radS2-1 strains obtained from R. Malone. Growth and sporulation of cells. Cells were ordinarily pregrown in the acetate-containing presporulation medium (PSP) of Roth and Halvorson (34) [32]) and aprotinin (Sigma Chemical Co.) (13). When 5 x 109 cells or more were to be broken, the Bronwill homogenizer was used.…”

Section: Methodsmentioning

confidence: 99%

Developmental regulation of a sporulation-specific enzyme activity in Saccharomyces cerevisiae.

Clancy¹,

Smith²,

Magee³

1982

Mol. Cell. Biol.

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An alpha-glucosidase activity (SAG) occurs in a/alpha Saccharomyces cerevisiae cells beginning at about 8 to 10 h after the initiation of sporulation. This enzyme is responsible for the rapid degradation of intracellular glycogen which follows the completion of meiosis in these cells. SAG differs from similar activities present in vegetative cells and appears to be a sporulation-specific enzyme. Cells arrested at various stages in sporulation (DNA replication, recombination, meiosis I, and meiosis II) were examined for SAG activity; the results show that SAG appearance depends on DNA synthesis and some recombination events but not on the meiotic divisions.

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Section: Methodsmentioning

confidence: 99%

Developmental regulation of a sporulation-specific enzyme activity in Saccharomyces cerevisiae.

Clancy¹,

Smith²,

Magee³

1982

Mol. Cell. Biol.

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“…The trypsin-inhibiting capacity was measured us ing the synthetic chromogcnic substrate a-N-bcnzoyl-DL-arginine-p-nitroanilide [8] as previously described [1], One inhibiting unit (IU) corresponds to I enzyme unit (turnover rate 1 pmol of substrate/min) and ap proximately to an inhibition of 0.4 mg porcine trypsin (Novo Industries, Copenhagen, Denmark). Negative values of trypsin-inhibiting capacity were registered as trypsin activity.…”

Section: Analysesmentioning

confidence: 99%

Proteinase Inhibitors in the Gastrointestinal Tract, Pancreas and Liver during Fetal and Postnatal Development of the Pig

Ohlsson¹,

Weström²,

Karlsson³

1986

Neonatology

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The occurrence and types of proteinase inhibitors were studied in the digestive system during the fetal and postnatal development of the pig. The protein concentration, the total trypsin-inhibiting capacity and the levels of the individual proteinase inhibitors, α₂-macroglobulin f (α₂Mf), α₂-macroglobulin s (α₂Ms), α₁-protease inhibitor (α₁PI) and α₂-antitrypsin (α₂AT) quantified by using electroimmunoassay, were assayed in stomach and intestinal contents, in homogenates of the stomach and intestinal mucosa, and in the pancreas and liver. The results showed that during porcine ontogeny high amounts of proteinase inhibitors are present in the digestive system. During the fetal period, the most outstanding characteristic was the high levels of α₁PI and α₂AT, in contrast to the low levels of the α₂-macroglobulins. Furthermore, the trypsin-inhibiting capacity and the levels of α₁PI and α₂AT showed in most cases a statistically significant decrease during the fetal period (12–36 cm crown-to-rump length). In the neonatal period, 0–96 h after birth, the levels of the individual inhibitors were rather constant, but a significant decrease to low levels of both trypsin inhibition and the individual inhibitors was observed in the adult pig. Trypsin activity was found in approximately half of the pancreas homogenates from the late fetal period and in newborn pigs before they began to suckle. The physiological function of the proteinase inhibitors observed in the digestive system during porcine ontogeny is probably to protect against precocious proteolytic degradation by the formation of inactive enzyme/inhibitor complexes.

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“…The inhibiting capacity of centrifuged (defatted) human milk against bovine trypsin was determined using BAPNA as substrate (6,12). Figure 1 shows the trypsin inhibiting activity in porcine colostrum, in human milk from the 2nd day, and in serum and urine from the 2-day-old infant.…”

Section: Quantitative Determination Of Trypsin-inhibiting Activitymentioning

confidence: 99%

Protease Inhibitors in Human Milk

Lindberg

1979

Pediatr Res

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Summarystandard serum for the measurements of the concentration of a,-Protease inhibitors (inhibiting trypsin, chymotrypsin, and elastase) were demonstrated in human milk from birth to 4 months after delivery. No pepsin inhibitor was found. The protease inhibitors were localized in the al-region-inhibiting trypsin, chymotrypsin, and elastase-and in a more cathodal region-inhibiting chymotrypsin-in agarose gel electrophoresis of human milk. alantitrypsin and antichymotrypsin were demonstrated by crossed immunoelectrophoresis. Electroimmunoassay showed the concentration of a,-antitrypsin in 1st day milk to be 109% and the concentration of antichymotrypsin was 116% of that of adult serum. The concentrations d&;eased during the 1st wk; from 1 wk to 4 months they were 1.6% for a,-antitrypsin and 3.84% for antichymotrypsin of those of adult serum. One ml of human milk from the first 3 days inhibits, by enzymatic methods, 0-150 pg (mean value, 70 pg) trypsin. Milk from 1 week after delivery and later inhibits 0-65 pg (mean value, 38 pg) trypsin per ml.

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Über Proteaseinhibitoren, I. Isolierung und Charakterisierung des Trypsininhibitors aus Pankreasgewebe und Pankreassekret vom Hund

Cited by 81 publications

References 0 publications

Developmental regulation of a sporulation-specific enzyme activity in Saccharomyces cerevisiae.

Developmental regulation of a sporulation-specific enzyme activity in Saccharomyces cerevisiae.

Proteinase Inhibitors in the Gastrointestinal Tract, Pancreas and Liver during Fetal and Postnatal Development of the Pig

Protease Inhibitors in Human Milk

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