Chicken pepsinogens and pepsins. Their isolation and properties

St, Donta; H, Van Vunakis

doi:10.1021/bi00816a006

Cited by 35 publications

(17 citation statements)

References 30 publications

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“…The degree of hydrolysis depended on several factors ( [3,10,22,28]. Chicken pepsin is more efficient in hydrolysing typical substrates such as haemoglobin and less active in clotting milk than pig pepsin [ 10,22].…”

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Comparison of pig and chicken pepsins for protein hydrolysis

Crévieu-Gabriel¹,

Gomez²,

Caffin³

et al. 1999

Reprod. Nutr. Dev.

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-The aim of the present study was to compare the degree of proteolysis with pig (PP) and chicken (CP) pepsins in order to find out whether PP can be used instead of CP to simulate gastric hydrolysis in the chicken. First, the pH activity profile of the two pepsins was compared using three substrates. For haemoglobin, CP showed a slightly higher optimal pH than PP, 2.5-3 and 2, respectively. For two plant protein sources (peas, wheat), the optimal pH was similar for the two enzymes, about pH 1.5. For the three substrates tested, CP exhibited a high level of activity over a broader pH range than PP. Second, the susceptibility of the two plant proteins to hydrolysis by each of the two pepsins was studied at pH levels near the chicken gastric pH (1.5-3.5). For PP, pea proteins were hydrolysed more than wheat ones, while, for CP, the hydrolysis was dependent on pH. Therefore (1,5). Alors qu'avec la PP les protéines de pois ont été mieux hydrolysées que celles du blé, dans le cas de la CP le résultat dépend du pH. La classification des deux sources de protéines étudiées dépend donc de l'origine animale de

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“…Chicken pepsin is more efficient in hydrolysing typical substrates such as haemoglobin and less active in clotting milk than pig pepsin [ 10,22]. The Indeed, the mean transit time in the chicken gizzard is about 20 and 50 min for soluble and insoluble markers, respectively [32], whereas it is about 3 and 13 h, respectively, in the pig stomach [7].…”

mentioning

confidence: 99%

Comparison of pig and chicken pepsins for protein hydrolysis

Crévieu-Gabriel¹,

Gomez²,

Caffin³

et al. 1999

Reprod. Nutr. Dev.

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“…The heterogeneity of gastric zymogens has been established by chromatographic and electrophoretic studies of extracts of pig stomach (Lee & Ryle, 1967), human gastric mucosa (Turner et al, 1970), chicken stomachs (Donta & Van Vunakis, 1970) and dogfish stomachs (Merrett et al, 1969). Four pepsinogens have been separated from bovine fundic mucosa by chromatography on hydroxyapatite at pH7.3 (Meitner & Kassell, 1971).…”

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Fractionation and isolation of the multiple forms of prorennin (prochymosin)

Asato

Rand

1972

Biochemical Journal

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The heterogeneity of prorennin was studied by chromatography on DEAE-cellulose and microgranular DEAE-cellulose columns, as well as by polyacrylamide-gel electrophoresis. Prorennin prepared by alum treatment, salting-out and chromatography was resolved into three components by a compound gradient of sodium phosphate on microgranular DEAE-cellulose. Polyacrylamide-gel electrophoresis confirmed the chromatographic results, but crystalline rennin was shown to consist of four bands. When prorennin was isolated directly by chromatography, four zymogen components were resolved on microgranular DEAE-cellulose with a modified compound gradient of sodium phosphate. Polyacrylamide-gel electrophoresis confirmed the existence of four multiple forms of prorennin as well as homogeneity of the chromatographic fractions.

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“…Peptic isozymes have been described in other vertebrates, generally having different pH optima, as well as different resistance to denaturation with alkali (Buchs, 1971). Peptic isozymes have been described in fishes (Merrett et al, 1969), birds (Donta & van Vunakis, 1970), man (Etherington & Taylor, 1969;Samloff & Townes, 1970;Samloff, 1971) and other mammals (Chiang et al, 1967;Chow & Kassel, 1968). Nevertheless, caution must be exercised before asserting the existence of isozymes.…”

Section: Peptic Proteolysismentioning

confidence: 99%

Gastric function in Caiman crocodilus (Crocodylia: Reptilia)—II. Effects of temperature on pH and proteolysis

Diefenbach

1975

Comparative Biochemistry and Physiology Part A: Physiology

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In Caiman crocodilus, the pH of the gastric secretions during digestion may reach 1.2 in specimens kept between 20 and 30°C. C. crocodilus feeds and digests at 15°C, but the pH of gastric secretions did not drop below 1-8. 2. The gastric secretion increased in rate and hydrochloric acid concentration after injections of histamine (400 t~g/kg body weight, given in four hourly doses). The rate increased from 0.05 ml/kg, hr (resting rate, at 20°C) up to an average of 0.66 ml/kg, hr, at 30°C. 3. There is a latent period of 4-8 hr before the effects of histamine can be detected in tests carded out at 20, 25 and 30°C. 4. Peptic proteolysis of gastric secretions has pH optima in the range 2.0-2.6, when carded out at 25°C, using the hemoglobin method of Anson & Mirsky. 5. There were instances of more than one pH optimum for proteolysis, suggesting the occurence of isozymes. 6. Inside the range in which C. crocodilus feeds and digests, peptic proteolysis has an average Qlo of 1.62 (between 15 and 25°C) and of 1.50 (between 25 and 35°C). 7. In animals maintained at 25°C peptic proteolysis was highest at 24-48 hr after feeding.

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Chicken pepsinogens and pepsins. Their isolation and properties

Cited by 35 publications

References 30 publications

Comparison of pig and chicken pepsins for protein hydrolysis

Comparison of pig and chicken pepsins for protein hydrolysis

Fractionation and isolation of the multiple forms of prorennin (prochymosin)

Gastric function in Caiman crocodilus (Crocodylia: Reptilia)—II. Effects of temperature on pH and proteolysis

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