Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P00790 (PGA)
 2,475 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Pepsin-solubilized bovine corium collagen was reconstituted by rapid neutralization in dilute phosphate buffer at temperatures ranging from 10 degrees C-25 degrees C. The resultant fibrils were harvested by centrifugation and resuspended in physiological buffer to a constant protein concentration. The optical density of such suspensions, measured at 410 nm in a 1 mm path length cuvette, exhibited a strong inverse correlation with temperature of fibrillogenesis. The absorbance values of fibrillar suspensions prepared from intact collagen were greater than those observed with suspensions prepared from pepsin-solubilized collagen under similar conditions and demonstrated a reduced dependence on temperature of fibril assembly. The nature of the variation in opacity of fibrillar suspensions prepared from pepsin-solubilized material was further investigated using transmission electron microscopy, trypsin sensitivity, SDS gel electrophoresis and polarimetry. Reconstitution conditions that favored more rapid precipitation (e.g., higher incubation temperatures) tended to produce fibril suspensions of lower opacity (translucent). These translucent suspensions exhibited fibrils that were small in diameter when compared to fibril suspensions of higher opacity. Translucent preparations also contained higher levels of a trypsin sensitive, early melting component and displayed a higher proportion of peptides migrating faster than alpha 2(I) on SDS polyacrylamide gels. Collagen preparations depleted of the early melting component continued to demonstrate the correlation between increased temperature and decreased fibrillar opacity, suggesting that the two phenomena were independent. It is proposed that the unstable components are nicked or shortened collagen helices, presumably generated by pepsinization or the action of endogenous proteases of the bovine corium, which are differentially incorporated into fibrils depending on the conditions of fibril assembly.
 ...
PMID:Collagen fibrillogenesis in vitro: a characterization of fibril quality as a function of assembly conditions. 392 70

Both the triple-helical and denatured forms of nonfibrillar bovine dermal type I collagen were tested as substrates for the catalytic subunit of cAMP-dependent protein kinase in an in vitro reaction. Native, triple-helical collagen was not phosphorylated, but collagen that had been thermally denatured into individual alpha chains was a substrate for the protein kinase. Catalytic subunit of cAMP-dependent protein kinase phosphorylated denatured collagen to between 3 to 4 mol of phosphate/mol of (alpha 1(I)2 alpha 2(I). Pepsin-solubilized and intact collagens were phosphorylated similarly, as long as each was in a nonhelical conformation. The first 2 mol of phosphate incorporated into type I collagen by the protein kinase were present in the alpha 2(I) chain. The alpha 1(I) chain was only phosphorylated during long incubations in which the stoichiometry exceeded 2 mol of phosphate/mol of (alpha 1(I)2 alpha 2(I). Phosphoserine was the only phosphoamino acid identified in collagen that had been phosphorylated to any degree by the protein kinase. The 2 mol of phosphate incorporated into the alpha 2(I) chain were localized to the alpha 2(I)CB4 cyanogen bromide fragment. The catalytic subunit of cAMP-dependent protein kinase phosphorylated denatured pepsin-solubilized collagen with a Km of 8 microM and a Vmax of approximately 0.1 mumol/min/mg of enzyme. Denatured, but not triple-helical, type I collagen was also phosphorylated by cGMP-dependent protein kinase, although it was a poorer substrate for this enzyme than for the cAMP-dependent protein kinase. Collagen was not a substrate for phospholipid-sensitive Ca2+-dependent protein kinase. These results suggest the potential for nascent alpha chains of type I collagen to be susceptible to phosphorylation by cAMP-dependent protein kinase in vivo prior to triple-helix formation. Such a phosphorylation of collagen could be relevant to the action of cAMP to increase the intracellular degradation of newly synthesized collagen.
 ...
PMID:In vitro phosphorylation of type I collagen by cyclic AMP-dependent protein kinase. 395 36

Human umbilical blood vessels have the ability to close spontaneously following delivery at term. It has been suggested that prostaglandins may have a possible physiological role in its closure. This study investigates the effects of 6 naturally occurring prostaglandins (A1, A2, B1, B2, E2, F2a) on the umbilical blood vessels. Umbilical cords were collected from cases of normal spontaneous vaginal deliveries and cesarian section at term. A total of 41 strips of umbilical arteries and 26 strips of umbilical veins from 24 cords were used. A 4-point bioassay method was used to compare the potency of prostaglandins A1, A2, B1 and F2a with PGE2. The effect of Polyphloretin Phosphate (PPP) on prostaglandin-induced contractions was studied on umbilical artery strips from 12 cords. The 6 prostaglandins exerted a stimulant effect on the isolated strips of human umbilical arteries. Prostaglandin B2 was the most potent compound on the umbilical vein, followed by PGA2. PPP in the concentration range of 10 to 40 mcg/ml completely eliminated the responses of PGE2, F2a, A1, A2, and B1. Responses to PGB2 were considerably but not completely abolished. PPP (up to 40 mcg/ml) did not affect contractions induced by 5-hydroxytryptamine, suggesting the presence of discrete receptor sites in the blood vessels for different pharmacologically active compounds. This is the first report of the constrictor effect of PGA and PGB compounds. These naturally occuring prostaglandins with high potencies (compared with other prostaglandins and other vasoactive substances) may play a role in spontaneous closure of umbilical vessels. PGE1, E2, F1 and F2a are found in umbilical blood vessels obtained at term.
 ...
PMID:Effect of prostaglandins A1, A2, B1, B2, E2 and F2 alpha on human umbilical cord vessels. 445 25

Methods are described for the isolation and purification of pepsin D, an enzyme which accounts for about 10% of the enzymic activity in commercial preparations of pepsin. Pepsin D is similar to pepsin in having a molecular weight of about 35000, the same C-terminal amino acid sequence, and an N-terminal isoleucine residue. It differs in having no phosphate residue. Pepsin D is similar to pepsin in its ability to digest haemoglobin, acetyl-l-phenylalanyl-l-di-iodotyrosine and gelatin but it is twice as active as pepsin in the clotting of milk. It has the same specificity as pepsin in its action on the B-chain of oxidized insulin. It is probable that the pepsin D in commercial preparations of pepsin arises from the activation of gastric pepsinogen D.
 ...
PMID:Pepsin D. A minor component of commercial pepsin preparations. 486 Jun 38

Camel (Camelus dromedarius) pepsins were precipitated from the extract of the fundic gastric mucosa by ammonium sulfate between 35 and 80% saturation. DEAE--cellulose chromatography of this fraction produced two isoenzymes, I and II, which were further purified to homogeneity on sephadex G-100. Their Km with N-acetyl-L-phenylalanyl-diiodotyrosine were 0.10 and 0.90 mM, and their molecular weights which were determined on sodium dodecylsulfate gel electrophoresis exhibited 35,500 and 34,700, respectively. The two pepsins were essentially free of carbohydrates, but contained 0.3 and 1.0 mol of organic phosphate per 1 mol of protein, respectively. The apparent mobilities of the phospho- and dephosphoforms of each pepsin were indifferent in polyacrylamide gel electrophoresis at pH 8.9. The N-terminal residues of pepsins I and II were found to be alanine and leucine, respectively. Pepsin I was inactivated at a faster rate than that of pepsin II at pH 8 and 0 degrees C, and at pH 7.5 and 37 degrees C; but both were denatured under these conditions. The properties of these enzymes are compared with those of other mammalian and avian pepsins.
 ...
PMID:Isolation and characterization of camel pepsins. 614 Oct 27

The tensile strengths of poly(glycolic acid) (PGA) sutures immersed in buffered and unbuffered aqueous media were compared. The media used were an unbuffered physiological saline solution (pH = 5.0) and a phosphate-buffered physiological saline solution (pH = 7.4). PGA samples were immersed for various periods in each medium, and kept at 37 +/- 1 degree C in a constant temperature oven. The tensile strengths of the specimens were tested immediately after removal from the medium. Stress-strain curves of the specimens were expressed in terms of the stress unit "tenacity," commonly used in the study of fibrous polymers; it is an appropriate unit for materials of fibrous nature. These stress-strain curves were investigated as functions of buffering and duration of immersion. Degradation reduced the tensile strength of PGA more in the buffered saline solution than in the unbuffered. This higher rate of degradation in the buffered solution might be due to the presence of Na2HPO4, which removed the degradation products, shifted the reaction toward increased hydrolosis, and accelerated the loss of tensile strength in the PGA. A continuous decrease in the pH of the unbuffered solution supports this explanation. Tied-chain segments of macromolecules, a theory widely used in the study of mechanical strength of fibrous polymer may be the key to a comprehensive description of the degradation phenomenon of PGA.
 ...
PMID:An in-vitro study of the effect of buffer on the degradation of poly(glycolic acid) sutures. 629 20

In 15 anesthetized rabbits the reflex changes in arterial pressure, heart rate and respiratory rate in response to injections of bradykinin inorganic phosphate and prostaglandins into femoral artery have been studied. Intraarterial injection of bradykinin produced a reflex fall in arterial pressure, bradycardia and tachypnea. The latency of response ranged from 6 to 7 sec. The threshold dose was about 50 ng. This effect was accompanied by a consistent increase in the afferent discharge in the saphenus nerve. Isotonic mixtures of Na2HPO4 and NaH2PO4 at pH 7, PGE1, PGE2, and PGA, when injected into femoral artery even in high doses, failed to produce any significant cardiocirculatory or respiratory reflex responses. Infusion of PGE1 (1 ug/min) into femoral artery, although inactive by itself, enhanced the reflex effect of bradykinin.
 ...
PMID:[Comparative study of cardiocirculatory response and respiratory reflex to the injection of bradykinin, inorganic phosphates and prostaglandins into the femoral artery]. 730 10

Pepsin (3.6 nmol) was detected by the following three-step procedure: (i) reaction with a 20-fold molar excess of BO-IMI (a fluorophore containing a reactive imidazole group) in the presence of a 150-fold molar excess of 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) and 2% sodium dodecyl sulfate; (ii) gel filtration (spin column) to remove most of the residual BO-IMI; and (iii) capillary electrophoresis with laser-induced fluorescence detection. For the latter step, 8.5 x 10(-7) of the original sample was injected. BO-IMI/EDC targets phosphomonoesters and does not label albumin (prior knowledge). Progressive dephosphorylation of pepsin with acid phosphatase reduced its labeling with BO-IMI. Thus, the BO-IMI, as intended, labels the phosphate group on pepsin. Such BO-IMI labeling should be useful in general for studying phosphoproteins and phosphopeptides.
 ...
PMID:Phosphate-specific fluorescence labeling of pepsin by BO-IMI. 750 26

An in vitro method was developed to predict inorganic P release from maize-soyabean poultry feeds containing supplemental phytase (EC 3.1.3.8), and to quantify the effect of acid phosphatase (EC 3.1.3.2), fungal protease (EC 3.4.23.6) and Aspergillus niger cellulase (EC 3.2.1.4) on phytate dephosphorylation. Pepsin (EC 3.4.23.1) and pancreatin digestion periods were preceded by a 30 min pre-incubation at pH 5.25 to simulate digestion in the crop of poultry. Pancreatin digestion was carried out in dialysis tubing, with a ratio of about 1:25 (v/v) between the digesta and dialysing medium, to simulate gradient absorption from the duodenum. The feed:water ratio was kept within physiological limits and a constant proportion of feed weight to digestive enzymes was maintained. There was a linear response to increasing dosages of phytase up to 1000 phytase units (FTU)/kg feed, and to increasing phosphate concentration in feeds. In vivo validation was performed with growing turkeys (1-3 weeks) fed on diets containing 12 g Ca/kg and 0, 500 or 1000 FTU phytase/kg in a factorial arrangement with 0, 1, 2 or 3 g supplemental phosphate/kg (from KH2PO4). After a simple transformation (variable/in vitro P = f (in vitro P)), amounts of P hydrolysed from feed samples by in vitro digestions correlated with 3-week body-weight gain (R 0.986, P < 0.0001), toe ash (R 0.952, P < 0.0001), feed intake (R 0.994, P < 0.0001) and feed efficiency (R 0.992, P < 0.0001). The dephosphorylating ability of phytase in vitro was significantly enhanced (P < 0.05) by the addition of acid phosphatase. Fungal acid protease and Aspergillus niger cellulase also enhanced the dephosphorylation process in vitro.
 ...
PMID:An in vitro procedure for studying enzymic dephosphorylation of phytate in maize-soyabean feeds for turkey poults. 754 27

A three-step in vitro procedure was developed to estimate intestinal digestion of proteins in ruminants. Dacron bags containing feed samples were suspended in the rumen for 16 h. Residue containing 15 mg of N after ruminal exposure was incubated for 1 h in 10 mL of a .1 N HCl solution containing 1 g/L of pepsin. After incubation, pH was neutralized with .5 mL of 1 N NaOH and 13.5 mL of a pH 7.8 phosphate buffer containing 37.5 mg of pancreatin were added to the solution and incubated at 38 degrees C. After a 24-h incubation, 3 mL of a 100% (wt/vol) trichloroacetic acid solution were added to precipitate undigested proteins. Preincubation of samples in the rumen did not affect (P > .05) pepsin-pancreatin digestion of residual CP in soybean meal (SBM), corn gluten meal (CGM), and blood meal (BM) and reduced (P < .05) pepsin-pancreatin digestion of residual CP in hydrolyzed feather meal (HFM), fish meal (FM), and meat and bone meal (MBM) (80 vs 70, 88 vs 81, and 82 vs 56%, respectively, for nonruminal vs ruminal preincubation). Pepsin digestion before pancreatin digestion increased (P < .05) CP digestion of all proteins tested by a mean of 23 percentage units. The pancreatin digestion step was validated using 34 duodenal samples from which small intestinal CP digestion was determined in vivo. The regression equation of in vivo estimates on pancreatin digestion had an r value of .91 (P < .001).(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:A three-step in vitro procedure for estimating intestinal digestion of protein in ruminants. 766 77


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>