scholarly journals Amino acid immunoreactivity in normal human retina and after brachytherapy

2013 ◽  
Vol 96 (5) ◽  
pp. 504-507 ◽  
Author(s):  
Clairton F de Souza ◽  
Monica L Acosta ◽  
Philip J Polkinghorne ◽  
Charles NJ McGhee ◽  
Michael Kalloniatis
Keyword(s):  
Amino Acid ◽  
Human Retina ◽  
Normal Human

Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

1993 ◽  
Vol 51 ◽  
pp. 388-389
Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett
Keyword(s):  
Amino Acid ◽  
Natriuretic Peptide ◽  
Vascular Tone ◽  
Cardiac Tissue ◽  
Ring Structure ◽  
Terminal Amino Acid ◽  
Amino Acid Peptide ◽  
Normal Human ◽  
Terminal Amino ◽  
The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

COMPOSITION EN ACIDES AMINES DE THYROGLOBULINES PROVENANT DE SUJETS EUTHYROIDIENS ET GOITREUX

1966 ◽  
Vol 53 (2) ◽  
pp. 297-302 ◽  
Author(s):  
Janine Bismuth ◽  
Marcel Rolland ◽  
Serge Lissitzky
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Human Thyroid ◽  
Thyroid Glands ◽  
Acides Aminés ◽  
Normal Human

ABSTRACT Amino acid composition of S19 thyroglobulin purified from three normal human thyroid glands, a hyperthyroid goiter, two hypothyroid familial goiters and a euthyroid goiter, has been determined. No significant differences in amino acid composition has been observed.

Hydroxylysine Glycosides in Human Urine

1971 ◽  
Vol 17 (8) ◽  
pp. 782-788 ◽  
Author(s):  
Marjorie F Lou ◽  
Paul B Hamilton
Keyword(s):  
Amino Acid ◽  
Human Urine ◽  
Bone Collagen ◽  
Molar Ratio ◽  
Collagen Turnover ◽  
Surgical Fusion ◽  
Cation Exchange Column ◽  
Normal Human ◽  
Effluent Stream ◽  
Pass Through

Abstract Hydroxylysyl-galactosyl-glucose (HGG) and hydroxylysyl-galactose (HG) were isolated from normal human urine and shown to be identical with hydroxylysine glycosides (OHLG's) whose structure had been elucidated in other laboratories. We devised a procedure for separating the OHLG's from many other urinary constituents by preliminary fractionation on a column of Sephadex. The OHLG's in the fractions so obtained were then isolated, uncontaminated with other ninhydrin-positive components, in a single pass through an analytical cation-exchange column equipped for splitting the effluent stream. In addition, a procedure was devised for determining as little as 10-9 mol of the OHLG's in 100 µl of filtrate (corresponding to 83.3 µl, of urine) on standard ion-exchange chromatographic amino acid analyzers. In normal adult urine, 1.5, µmol of each glycoside was present per 100 mg of creatinine; the molar ratio of HHG to HG was about 1.1 to 1.2. Each was present in plasma in about 400- to 500-fold smaller concentration than in urine. After surgical fusion of the spine, excretion of OHLG's increased and the ratio of HGG to HG decreased, changes we interpreted as indicating a more rapid bone-collagen turnover consequent to surgical damage.

Localization of putative amino acid neurotransmitters in the human retina

1980 ◽  
Vol 31 (6) ◽  
pp. 729-732 ◽  
Author(s):  
Dominic Man-Kit Lam ◽  
Joe G. Hollyfield
Keyword(s):  
Amino Acid ◽  
Human Retina ◽  
Amino Acid Neurotransmitters

Thrombin Activatable Fibrinolytic Inhibitor Modulation in Heparin Supplemented Plasma: Clinical Considerations.

Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 3998-3998
Author(s):  
Michelle Florian-Kujawski ◽  
Debra Hoppensteadt ◽  
Marianne Wilmer ◽  
Jawed Fareed
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Normal Individuals ◽  
Exact Function ◽  
Anticoagulant Drugs ◽  
Heparin Plasma ◽  
Normal Human ◽  
Tissue Factor Pathway ◽  
Clinical Considerations ◽  
Inhibition Of Thrombin

Abstract Thrombin activatable fibrinolytic inhibitor (TAFI) is a procarboxypeptidase that cleaves the arginine and lysine amino acid residues off the carboxyl terminus of fibrin strands rendering fibrin resistant to the digestive actions of plasmin. Anticoagulant drugs such as the heparins and antithrombin drugs (hirudin, angiomax, argatroban and ximelagatran) by virtue of their inhibition of thrombin and its complex formation with thrombomodulin can down regulate the functionality of TAFI. It is now known that there are several TAFI polymorphisms, but the exact function of each form of TAFI is unclear at this time. Heparin-antithrombin complex produces strong inhibition of thrombin and thrombin-thrombomodulin complex and thereby reduces the conversion of TAFI to TAFIa. However, despite anticoagulation some of the individuals do not exhibit decreased TAFI functionality. In order to determine if a population of normal healthy volunteers exhibits differences in TAFI functionality upon anticoagulation with heparin, plasma samples were divided into two aliquots; saline was added to one set and 2.5 U heparin was added to the second set. This resulted in a final concentration of 0.25 U of heparin, which mimics therapeutic levels. Functional TAFI levels were determined using a synthetic substrate based method from Pentapharm Inc. (Basel, Switzerland), functional tissue factor pathway inhibitor (TFPI) levels and anti-Xa levels were obtained using a chromogenic-based method from American Diagnostica (Stamford, CT). TAFI levels in the saline supplemented samples were 89.9 ± 16.0% (range; 58.9 – 126.7%) normal human pooled plasma (NHP). After heparin supplementation, TAFI levels were reduced to 45.6 ± 16.1% NHP (range: 24.2 – 139.8% NHP). Upon further analysis it was determined that 45 (33%) individuals showed TAFI levels > 50% NHP (62.7 ± 14.8; range: 51.5 – 139.8% NHP) and 16 (11.8%) showed TAFI levels > 65% NHP (74.0 ± 17.8; range: 65.1 – 139.8% NHP). The anti-Xa level in the heparin supplemented samples was 0.181 ± 0.179 U (range: 0 – 0.61 U/ml) of heparin showing that the samples were anticoagulated. Comparing the TAFI levels obtained from the individuals that showed higher than expected levels to the anti-Xa showed that although TAFI levels were higher, the anti-Xa levels showed that the individuals were adequately anticoagulated. Interestingly functional TFPI levels did not differ in the heparin supplemented (1.35 ± 0.4 U/ml) and controls (1.73 ± 0.6 U/ml). These studies suggest that normal individuals, and different patient populations, may respond differently to anticoagulation using heparin, as functional TAFI levels may remain normal even after heparinization. This may be due to TAFI polymorphism in some individuals that allow the activation of TAFI to TAFIa even though only a small amount of thrombin is present. It is also plausible that this form of TAFI is more readily activated by plasmin or that the TAFIa itself may be more efficient in cleaving the arginine and lysine amino acid residues from fibrin. This suggests that patients undergoing surgical procedures where anticoagulation with heparin is necessary may be at risk of a fibrinolytic deficit if their functional TAFI levels remain high. This may predispose these patients to impaired fibrinolysis leading to further complications.

A Study of Relations between the Absorption of Amino Acids, Dipeptides, Water and Electrolytes in the Normal Human Jejunum

1975 ◽  
Vol 49 (5) ◽  
pp. 401-408 ◽  
Author(s):  
D. B. A. Silk ◽  
P. D. Fairclough ◽  
Nicola J. Park ◽  
Annette E. Lane ◽  
Joan P. W. Webb ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Sodium Chloride ◽  
Human Subjects ◽  
Sodium Content ◽  
Sodium Chloride Solutions ◽  
Electrolyte Absorption ◽  
Wide Range ◽  
Osmotic Solution ◽  
Normal Human

1. A double-lumen perfusion technique was used to study the effect of a wide range of concentrations of the dipeptide glycyl-l-alanine and its constituent amino acids on water and electrolyte absorption from iso-osmotic solutions in the upper jejunum of normal human subjects. 2. There was no significant absorption of water and electrolytes from sodium chloride solution (150 mmol/l) but the presence of the dipeptide or its constituent amino acids stimulated water and electrolyte absorption. 3. Water absorption reached a peak at increasing amino acid and dipeptide concentrations and then tailed off. Our data suggest that the tailing off is not solely due to the diminished sodium content of the solutions. 4. During perfusion of the dipeptide-sodium chloride and amino acid-sodium chloride solutions solute and water were absorbed as an iso-osmotic solution. Analysis of the results indicates that this could occur at high dipeptide concentrations only if the majority of the dipeptide enters the cell intact.

Macromolecular markers in normal human retina and applications to human retinal disease

2016 ◽  
Vol 150 ◽  
pp. 135-148 ◽  
Author(s):  
Clairton F. de Souza ◽  
Lisa Nivison-Smith ◽  
David L. Christie ◽  
Phillip Polkinghorne ◽  
Charles McGhee ◽  
...  
Keyword(s):  
Retinal Disease ◽  
Human Retina ◽  
Normal Human

Amino Acid Sequence ofN-Terminal Peptide of Normal Human Serum Albumin

1971 ◽  
Vol 18 (3) ◽  
pp. 137-144 ◽  
Author(s):  
C.S. Liu ◽  
T. B. Shih ◽  
M.H. Hsin ◽  
R. Q. Blackwell
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Amino Acid Sequence ◽  
Serum Albumin ◽  
Human Serum ◽  
Normal Human Serum ◽  
Normal Human

Study of normal human retina cell by adaptive optics and pathological way

2005 ◽  
Author(s):  
Chuihui Jiang ◽  
Yanhua Chu ◽  
Wenji Wang ◽  
Gezhi Xu ◽  
Ning Ling ◽  
...  
Keyword(s):  
Adaptive Optics ◽  
Human Retina ◽  
Normal Human
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