Separation of pepsinogen I, pepsinogen II, and pepsinogen III from human gastric mucosa

Seijffers, Max J.; Segal, Harry L.; Miller, Leon L.

doi:10.1152/ajplegacy.1963.205.6.1106

Cited by 50 publications

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“…In fact, multiple human pepsins [29,54,50,10,52,11,12,3,6,31] and pepsinogens [55,49,16,7,13,62] were subsequently observed by various authors and classified according to their chromatographic and immunoelectrophoretic behaviour. By and by different nomenclatures based on different fractionation techniques, different reference systems as well as the utilization of gastric mucosa (pepsinogens) and of gastric juice (pepsins) led to a considerable confusion in the field of human gastric proteases [5].…”

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Charakterisierung von menschlichem Pepsin I gewonnen aus gereinigtem Magenpepsinogen I

Becker

Rapp

1979

Klin Wochenschr

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Immunochemical homogeneous human pepsinogen I-group (PgI) was purified by solid immunoadsorbent and by DEAE-chromatography from gastric mucosa. PgI contained five electrophoretic distinct bands at pH 8.2 but only four bands at pH 5.6. After acid activation human pepsin (PI) was separated from the inhibitory peptide by affinity chromatography using poly-L-lysine. Purified PgI contained 9-16% of the inhibitory peptide. The yield of PI was 64 to 85%. A 65% increase of specific activity was observed. PI demonstrated three bands in agar gel electrophoresis at pH 5.6. The pH range of PI was rather wide, showing two maxima at pH 2.0 and pH 3.0 with hemoglobin as substrate. Irreverisble inactivation of PI was observed at pH 7.0 and at a temperature of 60 degrees C. The Km-value of PI was 0.170 mmol as determined with N-acetyl-L-phenyl-alanyl-L-3,5 diiodotyrosine. The specific activity was 9.6 IU/mg (hemoglobin substrate) and 0.032 IU/mg (dipeptide substrate). Porc pepsinogen (PPg) and its activated pepsin (PP) was used for comparison. PP showed indentical elution patterns in affinity chromatography. In AEE PPg and PP demonstrated both two components at pH 5.6 with different electrophoretic mobilities. The pH optimum of PP was observed at pH 2.0. PP was slightly more sensitive in alkali and heat inactivation than human P. A higher Km-value of PP of 0.082 mmol and higher specific activity as compared to human PI was observed.

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confidence: 99%

Charakterisierung von menschlichem Pepsin I gewonnen aus gereinigtem Magenpepsinogen I

Becker

Rapp

1979

Klin Wochenschr

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“…15 Serum pepsinogens have been divided into three major groups labelled pepsinogen I (PgI), pepsinogen II (PgII) and 'slow-migrating-protease' (SMP): the PgI group has been most studied in relationship to peptic ulceration. These enzyme precursors are found in the chief and mucous neck cells of the mucosa of the gastric fundus and body, but not in the antral mucosa.29…”

Section: Pepsin Secretionmentioning

confidence: 99%

Mucus, pepsin, and peptic ulcer.

Venables¹

1986

Gut

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“…The first step in the enzymatic hydrolysis of dietary proteins occurs in the gastric lumen under the action of pepsins and HCI (Seijffers, Segal and Miller, 1963 …”

Section: Proteolytic Enzymesmentioning

confidence: 99%

Digestive enzymes in the germ-free animal

Corring¹,

Juste²,

Simoes-Nunes³

1981

Reprod. Nutr. Dévelop.

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Summary.The digestive physiology of the germ-free animal has a number of characteristics (cecal hypertrophy, slower small intestine cell renewal, slower gastric emptying and intestinal transit) which distinguish it from that of the conventional animal. If the germ-free model is to be used to determine the role of gastrointestinal microflora in the nutrition of the conventional animal, it is essential to complete the study of these characteristics by data on digestive enzymes in the germ-free. The present paper analyzes these data.There In general, the germ-free animal has some characteristics which should permit better utilization of the diet ingested. Measurements of apparent digestibility do not confirm this hypothesis since results obtained in germ-free and conventional animals of the same species are contradictory.The germ-free animal is certainly a very useful tool for studying the role of gastrointestinal microflora in the nutrition of its host. The large intestine contains the largest bacterial population (1 to 3.10 10 bacteria/g fresh contents) and the greatest number of microbial species in the gut (Ducluzeau and Raibaud, 1975 ;Schaedler, 1973). In some cases, bacteria may efficiently intervene in the digestive utilization of the diet ingested by the animal (R6rat, 1978).However, a number of experiments in the germ-free animal have shown that it cannot be considered simply as a conventional animal, deprived of gastrointestinal microflora, since certain characteristics of its digestive physiology distinguish it from the conventional animal (see reviews by Gordon et al.,1966 ;Combe et al., 1976). A knowledge of these characteristics is essential when determining the part due to bacteria in the digestion of an ingested diet.The germ-free state in rodents and lagormorphs leads to a substantial increase in cecal sac contents and size (Glimstedt, 1936 ;Wostmann and Bruckner-Kardoss, 1959 ;Wostmann, Bruckner-Kardoss and Knight, 1968 ;Pleasants, 1959 (Guenet et al., 1970). In the chicken, the rate of epithelial cell migration is lower in the germ-free than in the conventional state, but the relative differences are greater in the lower than in the upper intestine (Rolls, Turvey and Coates, 1978).Gastric emptying and small intestinal transit of the ingested food were found to be slower in the germ-free than in the conventional state. Six hours after a labelled test-meal, the cecum of the germ-free mouse retained a greater percentage of radioactivity than the cecum of the conventional animal, and the passage of the marker into the feces was slower (Abrams and Bishop, 1967). Gastrointestinal transit was also slower in the germ-free than in the conventional rat (Sacquet, Garnier and Raibaud, 1970 ;Riottot et al., 1980), and tended to be longer in germ-free rats fed irradiated diets than in those fed autoclaved diets (Riottot et al.,1980). The aim of the present review is to complete our knowledge of the characteristics of germ-free animal digestive physiology by analyzing data on digestive enzymes. These enzymes (p...

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Separation of pepsinogen I, pepsinogen II, and pepsinogen III from human gastric mucosa

Cited by 50 publications

References 0 publications

Charakterisierung von menschlichem Pepsin I gewonnen aus gereinigtem Magenpepsinogen I

Charakterisierung von menschlichem Pepsin I gewonnen aus gereinigtem Magenpepsinogen I

Mucus, pepsin, and peptic ulcer.

Digestive enzymes in the germ-free animal

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