Effects of acidity, cations and alcoholic fractionation on absorption of heparin from gastrointestinal tract

1976 ◽  
Vol 54 (4) ◽  
pp. 613-617 ◽  
Author(s):  
T. K. Sue ◽  
L. B. Jaques ◽  
E. Yuen
Keyword(s):  
Gastrointestinal Tract ◽  
Citric Acid ◽  
Blood Clotting ◽  
Molecular Size ◽  
Systemic Circulation ◽  
Anticoagulant Effect ◽  
Distilled Water ◽  
Simultaneous Administration ◽  
Factor X ◽  
Molecular Weight Fractions

Heparin was introduced into the stomach or duodenum of mice separately in doses of ca, 250 mg/kg. A slight anticoagulant effect in the systemic circulation was detected in whole blood clotting times and factor X inhibition. In contrast to most drugs, more heparin was absorbed from the stomach than from the intestine. Suppressing ionization of heparin by simultaneous administration of acid resulted in improved absorption of heparin from the small intestine. Heparin was separated with ethanol into five molecular weight fractions: I, 17 000; II, 13 200; III, 10 800, IV, 8 700; and V, 6 700. Each was introduced into the duodenum of mice with citric acid. The maximum hypocoagulability was produced with fraction IV. When administered in distilled water instead of in citric acid, this heparin fraction did not produce an anticoagulant effect. These studies demonstrated that improvement of heparin absorption from the gastrointestinal tract can be obtained by the combination of suppressing ionization and selecting molecular size.

Use Of Poly(L-Lysine)-Sepharose 4B For Isolation Of Vitamin K Dependent Factors From Human Plasma

1981 ◽  
Author(s):  
S F Mohammad ◽  
B Martin ◽  
H Y K Chuang ◽  
N C Sharma ◽  
R G Mason
Keyword(s):  
Ionic Strength ◽  
Blood Clotting ◽  
Sodium Citrate ◽  
Human Albumin ◽  
High Salt ◽  
Distilled Water ◽  
Factor X ◽  
Clotting Factors ◽  
Sepharose 4B ◽  
Blood Clotting Factors

Poly(L-lysine) (PLL; Mr=15,000-40,000) or human albumin was conjugated with Sepharose 4B-CNBr to obtain PLL-Sepha- rose 4B or albumin Sepharose 4B. When human citrated plasma was passed through a column (3×1 cm) of PLL-Sepharose 4B, it was observed that eluted plasma had a prolonged PTT time and further analysis showed that it was completely deficient in factors II, VII, IX, and X. Some loss of factors V, VIII, XI and XII was also noticed. Plasma passed through a column of albumin under identical conditions suffered no detectable loss of factors II, VII, IX and X. Loss of factors V, VIII, XI and XII was also reduced. Factors II, VII, IX and X that adsorbed to PLL-Sepharose 4B column did not elute from the column even after extensive washing (100 ml of 0.15 M NaCl containing 0.018 M sodium citrate in 5 ml aliquots). Immunoelectrophoretic examination of the eluate showed that it was essentially free of albumin indicating that the washing of the gel was satisfactory. Also, no other protein was detectable in the wash. Addition of 0.75 M NaCl containing 0.018 M sodium citrate to the washed gel resulted in the elution of factors II, VII, IX and X. Addition of the high salt eluate (after adjustment of ionic strength to 0.15 M NaCl with distilled water) to the plasma previously made deficient by passage through the PLL-Sepharose 4B column resulted in normalization of the PTT time. Subsequent analysis of the high salt eluate revealed that the recovery of various factors was: II=88%, VII=81%, IX=79% anl X=92%. Preliminary studies indicated also that the eluate from PLL-Sepharose 4B was apparently devoid of activated factor X. The possibility of other activated blood clotting factors being present in the PLL-Sepharose 4B eluate is currently under investigation.

Characterization of Recombinant Human Coagulation Factor XFriuli

1996 ◽  
Vol 75 (02) ◽  
pp. 313-317 ◽  
Author(s):  
D J Kim ◽  
A Girolami ◽  
H L James
Keyword(s):  
Catalytic Domain ◽  
Coagulation Factor ◽  
Molecular Size ◽  
Binding Pocket ◽  
Site Directed Mutagenesis ◽  
Bleeding Tendency ◽  
Factor X ◽  
Amino Terminal ◽  
Normal Plasma ◽  
Plasma Factor

SummaryNaturally occurring plasma factor XFriuli (pFXFr) is marginally activated by both the extrinsic and intrinsic coagulation pathways and has impaired catalytic potential. These studies were initiated to obtain confirmation that this molecule is multi-functionally defective due to the substitution of Ser for Pro at position 343 in the catalytic domain. By the Nelson-Long site-directed mutagenesis procedure a construct of cDNA in pRc/CMV was derived for recombinant factor XFriuli (rFXFr) produced in human embryonic (293) kidney cells. The rFXFr was purified and shown to have a molecular size identical to that of normal plasma factor X (pFX) by gel electrophoretic, and amino-terminal sequencing revealed normal processing cleavages. Using recombinant normal plasma factor X (rFXN) as a reference, the post-translational y-carboxy-glutamic acid (Gla) and (β-hydroxy aspartic acid (β-OH-Asp) content of rFXFr was over 85% and close to 100%, respectively, of expected levels. The specific activities of rFXFr in activation and catalytic assays were the same as those of pFXFr. Molecular modeling suggested the involvement of a new H-bond between the side-chains of Ser-343 and Thr-318 as they occur in anti-parallel (3-pleated sheets near the substrate-binding pocket of pFXFr. These results support the conclusion that the observed mutation in pFXFr is responsible for its dysfunctional activation and catalytic potentials, and that it accounts for the moderate bleeding tendency in the homozygous individuals who possess this variant procoagulant.

Kinetic Aspects of the Interaction of Blood-Clotting Enzymes

1968 ◽  
Vol 20 (01/02) ◽  
pp. 078-087 ◽  
Author(s):  
H. C Hemker ◽  
A. D Muller
Keyword(s):  
Vitamin K ◽  
Blood Clotting ◽  
Experimental Results ◽  
Factor X ◽  
Clotting Factors ◽  
Vitamin K Deficiency ◽  
K Deficiency

SummaryPIVKA, the circulating anticoagulant protein found in vitamin K deficiency can, on kinetical grounds, be recognized as an analogue of factor X. The existence of analogues of other vitamin K-dependent clotting factors cannot be ruled out, but need not be assumed to explain the experimental results.

scholarly journals Identification and Probiotic Potency Screening of Cellulolytic Bacilli Isolated from Fecal Pellets and Gastrointestinal Tract of Nypha Worm (Namalycastis rhodochorde), West Kalimantan, Indonesia

2021 ◽  
Vol 17 (2) ◽  
pp. 189-195
Author(s):  
TR Setyawati ◽  
AH Yanti ◽  
R. Kurniatuhadi
Keyword(s):  
Escherichia Coli ◽  
Gastrointestinal Tract ◽  
Organic Acids ◽  
Acid Tolerance ◽  
Distilled Water ◽  
Bacterial Identification ◽  
Bacterial Isolates ◽  
Fecal Pellets ◽  
West Kalimantan ◽  
E Coli

The bacterial isolates NrLtF1, NrLtF4, NrLtF5, and NrLtG2 isolated from fecal pellets and gastrointestinal tract of nypha worms (Namalycastis rhodochorde) have cellulolytic, proteolytic activity and produce organic acids. The four isolates have the potency to be developed as probiotics in nypha worm cultivation feed. This study aims to determine the probiotics potency and identify the species of NrLtF1, NrLtF4, NrLtF5, and NrLtG2 isolate based on 16srDNA sequence. The probiotic potency was carried out by the acid tolerance assays on distilled water and 0.3% acid bile media, and the antimicrobial testing against Escherichia coli (MF exp21.12). Bacterial identification was carried out by sequencing of 16sDNA sequence based on GeneBank data. The results showed that the bacterial isolates of NrLtF1, NrLtF4, NrLtF5, and NrLtG2 were able to grow on 0.3% distilled water and acid bile media. However, only the NrLtF4 and NrLtF5 inhibited E. coli (MF exp21.12) with halo zones 30 mm and 18 mm, respectively. Blasting results of the 16srDNA sequences showed that the NrLtF1, NrLtF4, NrLtF5, and NrLtG2 were closely related to Bacillus wiedmannii, Brevibacterium sediminis, Bacillus proteolyticus, and Bacillus paramycoides. The nypha worm bacterial isolates have the potency to be developed as probiotics in nypha worm culture.

Immune disorders of the gastrointestinal tract

2010 ◽  
pp. 2244-2256
Author(s):  
D.J. Unsworth
Keyword(s):  
Small Intestine ◽  
Gastrointestinal Tract ◽  
B Lymphocytes ◽  
Lamina Propria ◽  
Thoracic Duct ◽  
Lymphoid Tissue ◽  
Plasma Cells ◽  
Immunoglobulin A ◽  
Systemic Circulation ◽  
Lymphoid Follicles

The gastrointestinal tract is protected by gut-associated lymphoid tissue that provides an environment where interaction occurs between luminal antigen and specially adapted immune tissue in Peyer’s patches (small intestine only) or lymphoid follicles. T and B lymphocytes primed in the gut migrate into the systemic circulation via the thoracic duct but home preferentially to the lamina propria of the intestine. Plasma cells of the lamina propria secrete immunoglobulin A as a dimer linked by a joining peptide....

DICOUMAROL STUDIES: I. ORAL ADMINISTRATION OF SYNTHETIC DICOUMAROL TO VARIOUS CLASSES OF SHEEP AND CATTLE

1963 ◽  
Vol 43 (2) ◽  
pp. 344-352 ◽  
Author(s):  
J. H. Linton ◽  
B. P. Goplen ◽  
J. M. Bell ◽  
L. B. Jaques
Keyword(s):  
Vitamin K ◽  
Blood Clotting ◽  
Post Partum ◽  
Late Pregnancy ◽  
Cumulative Effects ◽  
Factor Vii ◽  
Factor X ◽  
Clotting Time ◽  
Sodium Bisulphite ◽  
Bull Calves

In one experiment 3 steers, 4 bull calves and 4 wether lambs were orally administered 2 milligrams dicoumarol per kilogram body weight and blood-clotting time measurements were made over a 4-day period. All animals responded to the dicoumarol but differences were evident between sheep and cattle; sheep were apparently more tolerant of the drug.The ’one-stage prothrombin’ test was more reliable and sensitive than the clotting tests employed for factor VII, factor X and prothrombin concentration.In a second experiment, 16 ewes in late pregnancy were fed rations containing 0 to 30 p.p.m. of synthetic dicoumarol and vitamin K3 as a cross treatment. Evidence of abnormal clotting power of ewe blood was observed in ewes fed diets containing 10 p.p.m. of dicoumarol. There was some indication of cumulative effects at this level after 32 days on test. At intake levels of 20 and 30 p.p.m. clotting times were affected more markedly and some ewes exhibited extended bleeding times after 2 to 4 weeks on test. No unusual hemorrhaging occurred at parturition. In general, the lambs’ blood did not reflect the pre- or post-partum dicoumarol intake of their mothers but a few lambs, as in the case of the ewes, exhibited low tolerance for dicoumarol without showing much disturbance in terms of clotting time. A large single oral dose of menadione sodium bisulphite demonstrated the effectiveness of vitamin K3 as an antidote. However, vitamin K3 as a ration supplement at 12 milligrams per pound feed failed to protect ewes against the effects of dicoumarol.

Assessment of protein permeability in normal human systemic circulation

1997 ◽  
Vol 273 (3) ◽  
pp. H1049-H1057 ◽  
Author(s):  
C. Shanholtz ◽  
P. White ◽  
S. Permutt ◽  
J. T. Sylvester ◽  
R. Brower
Keyword(s):  
Molecular Size ◽  
Normal Subjects ◽  
Systemic Circulation ◽  
Menstrual Phase ◽  
Edema Formation ◽  
Health And Disease ◽  
Normal Women ◽  
Forearm Circulation ◽  
Protein Permeability

Vascular permeability to oncotic agents is an important determinant of transvascular fluid flux (J) and systemic fluid balance. In this study, a technique was developed to measure protein reflection coefficients (omega) for albumin (Alb), immunoglobulin (Ig) G, and IgM in the intact human systemic circulation to evaluate the role of vascular protein permeability in health and disease. A mathematical model was developed to calculate omega in the forearm circulation from changes in venous hematocrit and protein concentration that occur during edema formation. Assumptions required for the model were validated in an initial set of experiments in normal subjects when edema was induced by inflating a pneumatic cuff on the upper arm. A second series of experiments assessed omega for Alb, IgG, and IgM in men (n = 7) and in women in the follicular (n = 5) and luteal (n = 4) phases of the menstrual cycle. There was an increasing trend in omega with molecular size in aggregated subjects [omega Alb = 0.81 +/- 0.12 (SE), omega IgG = 0.88 +/- 0.12, omega IgM = 0.92 +/- 0.18; P = 0.088]. These values were consistent with those obtained with in vitro preparations. omega values were lower in women in the luteal than in the follicular phase (P = 0.047). We conclude that the assumptions required for this model can be achieved in the intact forearm circulation and that there are menstrual phase-related differences in vascular protein permeability in normal women.

Two parallel prothrombin activator systems in Australian rough-scaled snake, Tropidechis carinatus

2005 ◽  
Vol 93 (01) ◽  
pp. 40-47 ◽  
Author(s):  
Md. Abu Reza ◽  
Sanjay Swarup ◽  
Manjunatha Kini
Keyword(s):  
Blood Coagulation ◽  
Blood Clotting ◽  
Cdna Sequence ◽  
Factor Xa ◽  
Coagulation Factor ◽  
Venom Gland ◽  
Factor X ◽  
Specific Expression ◽  
Life Saving ◽  
Sequence Encoding

SummaryIt is uncommon for similar pathways/systems to be involved in highly divergent functions within single organisms. Earlier, we have shown that trocarin D, a venom prothrombin activator, from the Australian rough-scaled snake Tropidechis carinatus, is structurally and functionally similar to the blood coagulation factor Xa (FXa). The presence of a haemostatic system in these snakes implies that they have two parallel prothrombin activating systems: one in the plasma, that participates in the life saving process of blood clotting and the other in their venom, where it acts as a toxin. Here, we report the complete cDNA sequence encoding the blood coagulation factor X (FX) from the liver of T. carinatus. Deduced T. carinatus FX sequence shows ~80% identity with trocarin D but ~50% identity with the mammalian FX. Our present study confirms the presence of two separate genes – one each for FX and trocarin D, that code for similar proteins in T. carinatus snake. These two genes have different expression sites and divergent uses suggesting that snake venom prothrombin activators have probably evolved by the duplication of the liver FX gene and subsequently marked for tissue-specific expression in the venom gland.

scholarly journals An endoprotease homologous to the blood clotting factor X as a determinant of viral tropism in chick embryo.

1990 ◽  
Vol 9 (12) ◽  
pp. 4189-4195 ◽  
Author(s):  
B. Gotoh ◽  
T. Ogasawara ◽  
T. Toyoda ◽  
N. M. Inocencio ◽  
M. Hamaguchi ◽  
...  
Keyword(s):  
Chick Embryo ◽  
Blood Clotting ◽  
Clotting Factor ◽  
Factor X ◽  
Viral Tropism ◽  
Blood Clotting Factor
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