Prebiotic Effects and Fermentation Kinetics of Wheat Dextrin and Partially Hydrolyzed Guar Gum in an Batch Fermentation System.

Scientific research demonstrates that two indigenous gut bacteria, and can contribute to human health. Although these bacteria can be consumed as probiotics, they can also be produced in the gut by bacteria, and are then called prebiotics. The primary objective of this study was to quantitatively analyze at the genus level how two dietary fibers, wheat dextrin (WD) and partially hydrolyzed guar gum (PHGG) changed the levels of these two gut bacteria at 12 and 24 h, via real time qualitative polymerase chain reaction (qPCR).

Fermentation profiles of wheat dextrin, inulin and partially hydrolyzed guar gum using an in vitro digestion pretreatment and in vitro batch fermentation system model.

This study investigated the fermentation and microbiota profiles of three fibers, wheat dextrin (WD), partially hydrolyzed guar gum (PHGG), and inulin, since little is known about the effects of WD and PHGG on gut microbiota. A treatment of salivary amylase, pepsin, and pancreatin was used to better physiologic digestion. Fibers (0.

Chronic dietary fiber supplementation with wheat dextrin does not inhibit calcium and magnesium absorption in premenopausal and postmenopausal women.

This placebo-controlled, randomized, crossover clinical study examined the effect of chronic wheat dextrin intake on calcium and magnesium absorption. Forty premenopausal and post menopausal women (mean ± SD age 49.9 ± 9.

Wheat dextrin, psyllium, and inulin produce distinct fermentation patterns, gas volumes, and short-chain fatty acid profiles in vitro.

Dietary fiber fermentation decreases luminal pH by the production of short-chain fatty acids (SCFAs). Additional proposed physiological benefits of fiber fermentation include decreased growth of pathogenic bacteria, increased mineral absorption, and serving as an energy source for the colon epithelium. This study examined three common fiber supplements--wheat dextrin (WD) (Benefiber, Novartis Consumer Health Inc.

Diaminoindanes as microsomal triglyceride transfer protein inhibitors.

The synthesis and biological activities of biarylamide-substituted diaminoindanes as microsomal triglyceride transfer protein (MTP) inhibitors are described. One of the more potent compounds, 8aR, inhibited both the secretion of apoB from Hep G2 cells and the MTP-mediated transfer of triglycerides between synthetic acceptor and donor liposomes with IC(50) values of 0.7 and 70 nM, respectively.

Human apolipoprotein B (apoB) mRNA: identification of two distinct apoB mRNAs, an mRNA with the apoB-100 sequence and an apoB mRNA containing a premature in-frame translational stop codon, in both liver and intestine.

Human apolipoprotein B (apoB) is present in plasma as two separate isoproteins, designated apoB-100 (512 kDa) and apoB-48 (250 kDa). ApoB is encoded by a single gene on chromosome 2, and a single nuclear mRNA is edited and processed into two separate apoB mRNAs. A 14.

Human proapolipoprotein A-I: development of an antibody to the propeptide as a probe of apolipoprotein A-I biosynthesis and processing.

In human plasma, apolipoprotein A-I is present as pro and mature isoproteins. The development of a highly specific antibody to the pro isoprotein of apoA-I has been difficult due to the close structural similarity between the pro and mature isoforms of apoA-I. To sermount this difficulty, a peptide was synthesized by the solid phase method which corresponded to the amino acid sequence present in the pro region of apoA-I.

Identification of a novel in-frame translational stop codon in human intestine apoB mRNA.

Human apolipoprotein (apo) B exists in plasma as two isoproteins designated apoB-100 and apoB-48. ApoB-100 (512 kDa) and apoB-48 (250 kDa) are synthesized by the liver and intestine respectively. Analysis of apoB cDNA clones isolated from a human intestinal cDNA library revealed that the intestinal apoB mRNA contains a new in-frame translational stop codon.

Human plasma apolipoprotein C-II: total solid-phase synthesis and chemical and biological characterization.

The complete amino acid sequence of human plasma apolipoprotein C-II (apoC-II) has been synthesized chemically by the solid-phase method using phenylacetamidomethyl-resin. All amino acids were coupled to the peptide-resin in the presence of 1-hydroxybenzotriazole; tert-butyloxycarbonyl-protected amino acids with the appropriate side-chain-protecting groups that are stable to the reaction conditions used in the solid-phase methodology were used. After cleavage and deprotection, the crude apoC-II was purified by ion-exchange chromatography and then by reverse-phase high-performance liquid chromatography.

Human liver apolipoprotein B-100 cDNA: complete nucleic acid and derived amino acid sequence.

Human apolipoprotein B-100 (apoB-100), the ligand on low density lipoproteins that interacts with the low density lipoprotein receptor and initiates receptor-mediated endocytosis and low density lipoprotein catabolism, has been cloned, and the complete nucleic acid and derived amino acid sequences have been determined. ApoB-100 cDNAs were isolated from normal human liver cDNA libraries utilizing immunoscreening as well as filter hybridization with radiolabeled apoB-100 oligodeoxynucleotides. The apoB-100 mRNA is 14.

Identification of low density lipoprotein receptor binding domains of human apolipoprotein B-100: a proposed consensus LDL receptor binding sequence of apoB-100.

The human liver apoB-100 gene cloned in the lambda gt-11 expression vector expresses fusion proteins reacting with apoB antibodies. A fusion protein induced from a apoB-lambda gt-11 clone reacted with apoB-100 monoclonal antibodies known to block the binding of LDL to the LDL receptor. The fusion protein contains an amino acid sequence domain enriched in positively charged residues which is complementary to the negatively charged amino acids present in the consensus LDL receptor binding domain.

Identification of sequence homology between human plasma apolipoprotein B-100 and apolipoprotein B-48.

The structural relationship between apolipoprotein B-100 (apo-B-100) and apolipoprotein B-48 (apo-B-48) has not been elucidated. A peptide fragment (MDB-18) of approximately 6 kDa was isolated from a tryptic digest of apo-B-100. The sequence of the first 22 amino acids of MDB-18 was determined by Edman degradation.

Amino acid sequence of human plasma apolipoprotein C-III from normolipidemic subjects.

The complete amino acid sequence of human plasma apolipoprotein C-III (apoC-III) isolated from normal subjects is described. ApoC-III is a linear polypeptide chain of 79 amino acids. Tryptic digestion of intact apoC-III produced 5 major peptides, while tryptic digestion of the citraconylated protein yielded two peptides.

The molecular biology of human apoA-I, apoA-II, apoC-II and apoB.

The application of molecular biology techniques has enabled us to determine the gene sequence, organization, transcription and processing of apolipoprotein genes. Consequently, new insights have been gained in the biosynthesis and processing of these proteins. In addition to apoA-I, apoA-II and apoC-III reported here, other apolipoprotein genes such as apoC-II and apoE genes were found to share common intron-exon organizations.

Human apolipoprotein B-100: cloning, analysis of liver mRNA, and assignment of the gene to chromosome 2.

Human apolipoprotein B-100 (apo B-100) is the major apolipoprotein of low density lipoproteins and the principal ligand for interaction with the low density lipoprotein receptor. The human apo B-100 gene has been inserted into a lambda gt-11 expression vector, and the apo B-100 cDNA clones have been identified by screening with a monospecific apo B-100 antiserum, by screening with synthetic oligonucleotides based on the amino acid sequence of peptides isolated from apo B-100, and by immunoblot analysis of the expressed protein with a monoclonal antibody to apo B-100. The complete nucleotide and derived-amino acid sequence of a 1.

Amino acid sequence of human plasma apolipoprotein C-II from normal and hyperlipoproteinemic subjects.

The complete amino acid sequence of human plasma apolipoprotein C-II isolated from normal individuals and a subject with type V hyperlipoproteinemia has been determined. Apo-C-II contains 79 amino acids with the following amino acid composition: Asp4, Asn1, Thr9, Ser9, Glu7, Gln7, Pro4, Gly2, Ala6, Val4, Met2, Ile1, Leu8, Tyr5, Phe2, Lys6, Arg1, Trp1. Cleavage of apo-C-II by cyanogen bromide produced three peptides designated as CB-1 (9 residues), CB-2 (51 residues), and CB-3 (19 residues).

Determination of glucocerebroside, sphingomyelin, free fatty acid and total lipid by thin-layer chromatography and charring-scintillation quenching.

A previously described method has been extended to various specific lipids of liver and brain. The basic method involves thin-layer chromatography followed by charring to reveal the bands. The intensity of each band is determined by suspending the silica gel in a radioactive scintillation gel and measuring the optically quenched activities.

A 2-phase liquid scintillation assay for glycolipid synthetases.

Glycolipid synthetases can be assayed conveniently by incubating the lipid substrate with the radiosugar-labeled nucleotide in a small plastic scintillation vial. At the end of the incubation period, water and perchloric acid are added, then n-butanol, then a toluene-based scintillation cocktail. The radioactive lipid partitions into the scintillation fluid, leaving excess sugar nucleotide in the aqueous phase.

Elevation of serum polyamines in malignant lymphomas and acute myeloid leukemia.

In a study of 89 cases of hematological cancers including 55 cases of Hodgkin's disease, 21 of non-Hodgkin lymphoma and 13 of acute myeloid leukemia, the serum total polyamines were considerably elevated (1.2-5.7 nmol/ml) as compared to observations on control values for eight healthy individuals (0.

Inactivation of (Na-++K-+)-stimulated ATPase by a cytotoxic protein from cobra venom in relation to its lytic effects on cells.

The mechanism of action of the cytotoxic protein P6 isolated from cobra venom (Naja naja) which shows preferential cytotoxicity particularly to Yoshida sarcoma cells has been studied by its effects on the membrane-bound enzyme (Na-++K-+)-ATPase (ATP phosphohydrolase, EC 3.6.1.