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Protein Loss (protein + loss)
Selected AbstractsBiochemical and Conformation Changes of Actomyosin from Threadfin Bream Stored in IceJOURNAL OF FOOD SCIENCE, Issue 3 2002J. Yongswawatdigul ABSTRACT: Biochemical and conformational changes of actomyosin stored in ice were investigated. The K-value of threadfin bream increased from 9% to 40% after storage for 12 d. Ca2+ -, EDTA-, Mg2+ -, and Mg2+ -Ca2+ -ATPase activities of actomyosin decreased, whereas Mg2+ -EGTA ATPase activities increased. Total SH content of actomyosin increased after 3 d and decreased thereafter. Surface hydrophobicity gradually increased within 6 d. Protein loss during washing increased with storage time. A significant reduction (50%) of breaking force of thrice-washed mince was observed in fish stored in ice for 6 d. There was no evidence of proteolysis of muscle proteins stored up to 9 d as shown with SDS-PAGE. [source] PEUTZ,JEGHERS POLYPOSIS WITH BLEEDING FROM POLYPS OF THE SIGMOID COLON SUCCESSFULLY TREATED BY LAPAROSCOPIC SURGERYDIGESTIVE ENDOSCOPY, Issue 1 2003Kazuhiro Yada We report a case of colonic bleeding complicating congestive heart failure in a patient with Peutz,Jeghers (P,J) polyposis successfully treated by laparoscopic surgery. A 49-year-old woman was admitted for severe cough and edema of the extremities. Chest X-ray revealed bilateral pleural effusion and cardiomegaly. Her cardiac function was within normal limits, but anemia and severe hypoproteinemia were observed. During the treatment, anal bleeding was observed. Endoscopic and radiographic examinations revealed hundreds of polyps from the duodenum to the rectum. 99mTc-diethylene triamine penta-acetic acid human serum albumin scintigraphy showed radiotracer collected in the sigmoid colon, the area having the most polyps. After some intestinal polypoid lesions were resected endoscopically, laparoscopy-assisted sigmoid colectomy and cecectomy were performed. In the postoperative course, she complained less about abdominal pain and her first flatus occurred on the third postoperative day. She recovered uneventfully. The anemia, hypoproteinemia, and congestive heart failure resolved and gastrointestinal bleeding has not been seen. It was thought that protein loss and hemorrhage due to the P,J polyposis caused congestive heart failure. When congestive heart failure is accompanied by gastrointestinal hemorrhage, it is important to consider hypoproteinemia due to gastrointestinal polyposis, such as that characterizing P,J syndrome. Laparoscopic surgery was very useful for the treatment of colonic bleeding. [source] Deletions removing the last exon of TACSTD1 constitute a distinct class of mutations predisposing to Lynch syndrome,HUMAN MUTATION, Issue 2 2009Marietta E. Kovacs Abstract Several different genetic alterations in the etiology of Lynch syndrome (hereditary nonpolyposis colorectal cancer [HNPCC]) are known, mostly point mutations and genomic rearrangements in 1 of at least 3 mismatch-repair (MMR) genes. However, no susceptibility factor has yet been identified in a significant part (30,50%) of clinicopathologically well-defined HNPCC families, suggesting the presence of other predisposing mechanisms. In a set of probands from 27 Lynch syndrome families who lacked evidence of a germline mutation in either the MSH2 or MLH1 gene, we performed genomic deletion screening with the use of multiplex ligation-dependent probe amplification (MLPA) and sequencing. We used immunohistochemistry (IHC) and microsatellite instability (MSI) analyses on samples of the probands of all families. Comparative analysis of mRNA transcripts was performed on blood leukocyte,derived samples from mutation carriers and noncarrier controls. We report that large germline deletions encompassing the last exons of the TACSTD1 gene, upstream of MSH2, cosegregate with the HNPCC phenotype in 19% (5/27) of families tested. The tumors of the carriers show high-level MSI and MSH2 protein loss. We show that these deletions, by removing the transcriptional termination sequences of the upstream gene, give rise to multiple TACSTD1/MSH2 fusion transcripts. Our results provide evidence that deletions removing the last exon of TACSTD1 constitute a distinct class of mutations predisposing to Lynch syndrome. Thus, analysis of the 3, region of the TACSTD1 gene should be included in the routine mutation screening protocols for HNPCC. Hum Mutat 30, 197,203, 2009. © 2009 Wiley-Liss, Inc. [source] Growth and feed utilization in two strains of gibel carp, Carassius auratus gibelio: paternal effects in a gynogenetic fishJOURNAL OF APPLIED ICHTHYOLOGY, Issue 2 2001Gibel carp (Carassius auratus gibelio Bloch) is a natural gynogenetic fish which requires sperm of the same or related species to activate egg development. The eggs of one gibel carp were divided into two batches. One batch was ,fertilized' with sperm from gibel carp (strain DD), and the other ,fertilized' with sperm from red common carp (Cyprinus carpio red variety) (strain DR). The juveniles were transferred to the laboratory 36 days post-hatch. Triplicate groups of each strain were fed a formulated diet at either 3% or satiation ration for 8 weeks. At both the restricted and satiation rations, specific growth rate was significantly higher in strain DR than in strain DD. At the 3% ration, there was no significant difference in feeding rate or feed conversion efficiency between the two strains. At the satiation ration, strain DR had a significantly lower feeding rate but higher feed conversion efficiency than strain DD. At the satiation ration, strain DR had a significantly lower intake protein, but higher recovered protein than strain DD. There was no significant difference in faecal protein loss between the two strains. At the 3% ration, strain had no significant effects on intake protein, faecal protein or recovered protein. Neither faecal energy loss nor recovered energy was affected by strain or ration. At both the 3% and satiation ration, final body contents of dry matter and lipid were significantly lower in strain DR than strain DD, while there was no significant difference in protein and energy content between the two strains at either ration level. The results suggested that gibel carp ,fertilized' with sperm of common carp grew faster than those ,fertilized' with sperm of gibel carp through increased feed conversion efficiency and protein retention. [source] Effects of NaCl Concentration on Salting-in and Dilution During Salting-out on Soy Protein FractionationJOURNAL OF FOOD SCIENCE, Issue 4 2006N. A. Deak ABSTRACT:, Glycinin and ,-conglycinin are the main storage proteins in soybeans that can be fractionated by using alkali extraction, SO2, salting-in with NaCl, salting-out by dilution and pH adjustment to produce a glycinin-rich fraction, a ,-conglycinin,rich fraction, and an intermediate fraction, which is a mixture of the two proteins. Two different strategies were employed to optimize the procedure to achieve high efficiency in recovering the ,-conglycinin,rich fraction. The first strategy was to optimize salting-in effects of NaCl, and the effects of NaCl concentration on the yields and purities of the protein fractions were investigated. The maximum protein yield of the ,-conglycinin,rich fraction was obtained at 500 mM NaCl, but at the expense of purity. The optimum NaCl concentration was 250 mM, at which good protein yield (18.5%) and purity (84.5%) were achieved. At higher NaCl concentrations, the protein yields of the intermediate fractions were significantly lower, and the protein loss in the whey fraction increased. The second strategy was to improve the salting-out step for the ,-conglycinin,rich fraction. At 0- and 0.5-fold dilution, the purities and yields of the ,-conglycinin,rich fractions were significantly lower than at 1.0- and 2.0-fold dilution. There were no differences in protein yields or purities when using 1.0- or 2.0-fold dilution. According to these results, the recommended NaCl concentration for the salting-in step is 250 mM and the dilution factor for salting-out is 1.0. [source] Chemical, biological and sensory evaluation of pasta products supplemented with ,-galactoside-free lupin floursJOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 1 2007Alexia Torres Abstract ,-Galactoside-free lupin flour has been used to supplement durum wheat semolina flour in order to increase the nutritive value of pasta products. Supplemented pasta products had a shorter cooking time, higher cooking water absorption, cooking loss and protein loss in water than control pasta prepared with only semolina. Sensory evaluation of cooked pastas showed that products supplemented with 80 g kg,1 of ,-galactoside-free Lupinus angustifolius var. Emir flour or with 100 g kg,1 of ,-galactoside-free Lupinus angustifolius var. Troll flour showed the same acceptability by panellists as the semolina pasta. These levels of supplementation were selected for further studies. The cooked ,-galactoside-free lupin/semolina pastas showed higher amounts of protein, dietary fibre, calcium, phosphorus, magnesium, zinc and antioxidant capacity than control pasta and a reasonable level of vitamin B1, vitamin B2 and vitamin E. Biological assessment of cooked pastas indicated that the true protein digestibility did not change after the fortification of semolina but protein efficiency ratio increased sharply in the pasta supplemented with ,-galactoside-free lupin flours (2.07 and 1.92 for Emir and Troll lupin varieties, respectively) in comparison with the control pasta (1.11). It is concluded that the ,-galactoside-free lupin flours are an adequate ingredient to improve the nutritional quality of pasta products without adding flatulent oligosaccharides. Copyright © 2006 Society of Chemical Industry [source] Intestinal Crypt Lesions Associated with Protein-Losing Enteropathy in the DogJOURNAL OF VETERINARY INTERNAL MEDICINE, Issue 3 2000M.D. Willard Six dogs were diagnosed with protein-losing enteropathy (PLE). There was no evidence of inappropriate inflammatory infiltrates or lymphangiectasia in multiple mucosal biopsies of the small intestine of 4 of the dogs. The 5th and 6th dogs had obvious lymphangiectasia and a moderate infiltrate of inflammatory cells in the intestinal mucosa. All 6 dogs had a large number of dilated intestinal crypts that were filled with mucus, sloughed epithelial cells, and/or inflammatory cells. Whether PLE occurs in these dogs because of protein lost from the dilated crypts into the intestinal lumen or whether the dilated crypts are a mucosal reaction due to another undetermined lesion that is responsible for alimentary tract protein loss is unknown. However, when large numbers of dilated intestinal crypts are present, they appear to be associated with PLE even if there are no other remarkable lesions in the intestinal mucosa. [source] Living liver donor death related to complications of myelomaLIVER TRANSPLANTATION, Issue 3 2009Emmanuel Melloul We report a donor death after right hepatectomy for living donor transplantation due to an undiagnosed myeloma. The 47-year-old donor, who was the 147th case performed in our department, was in excellent health without any abnormalities in the preoperative investigations. Despite an uneventful right hepatectomy without transfusion, the patient developed a partial thrombus of the inferior vena cava with a right proximal pulmonary trunk embolism on postoperative day 6. Subsequently, he developed multiorgan dysfunction leading to a coagulopathy, respiratory distress, and renal failure requiring hemodialysis and mechanical ventilation. This clinical scenario led us to suspect a hematological disorder. Immune electrophoresis showed a monoclonal peak of immunoglobulin G (8.7 g/L), a myelogram revealed an abnormally high level of dystrophic plasmocytes (more than 7%), and biopsies of salivary glands confirmed the diagnosis of immunoglobulin G kappa myeloma. The patient progressively deteriorated because of simultaneous hemorrhagic and infectious pulmonary complications resulting in septic shock. Despite an adequate combination of antimicrobial therapy and pleural drainage, the donor died on postoperative day 57 from multiple organ failure. This unusual cause of donor death after right hepatectomy reinforces the need for an extensive preoperative assessment. We advocate the addition of urinary protein loss and electrophoresis to the standard donor assessment protocol. Liver Transpl 15:326,329, 2009. © 2009 AASLD. [source] Control of the release of digestive enzymes in the larvae of the fall armyworm, Spodoptera frugiperdaARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY (ELECTRONIC), Issue 1 2010Digali Lwalaba Abstract There is a basal level of enzyme activity for trypsin, aminopeptidase, amylase, and lipase in the gut of unfed larval (L6) Spodoptera frugiperda. Trypsin activity does not decrease with non-feeding, possibly because of the low protein levels in plants along with high amino acid requirements for growth and storage (for later reproduction in adults). Therefore, trypsin must always be present so that only a minimal protein loss via egestion occurs. Larvae, however, adjust amylase activity to carbohydrate ingestion, and indeed amylase activity is five-fold higher in fed larvae compared to unfed larvae. Gut lipase activity is low, typical of insects with a high carbohydrate diet. A flat-sheet preparation of the ventriculus was used to measure the release of enzymes in response to specific nutrients and known brain/gut hormones in S. frugiperda. Sugars greatly increase (>300%) amylase release, but starch has no effect. Proteins and amino acids have little or no effect on trypsin or aminopeptidase release. The control of enzyme release in response to food is likely mediated through neurohormones. Indeed, an allatostatin (Spofr-AS A5) inhibits amylase and trypsin, and allatotropin (Manse- AT) stimulates amylase and trypsin release. Spofr-AS A5 also inhibits ileum myoactivity and Manse-AT stimulates myoactivity. The epithelial secretion rate of amylase and trypsin was about 20% of the amount of enzyme present in the ventricular lumen, which, considering the efficient counter-current recycling of enzymes, suggests that the secretion rate is adequate to replace egested enzymes. © 2009 Wiley Periodicals, Inc. [source] | |||||||||||||