scholarly journals A new case of deficiency of the R binder for cobalamin, with observations on minor cobalamin-binding proteins in serum and saliva

Blood ◽  
1982 ◽  
Vol 59 (1) ◽  
pp. 152-156
Author(s):  
R Carmel
Keyword(s):  
Molecular Weight ◽  
Alcohol Abuse ◽  
Incidental Findings ◽  
Clinical Presentation ◽  
Binding Capacity ◽  
Normal Serum ◽  
Serum Component ◽  
Almost All ◽  
Normal Controls ◽  
Low Serum

A patient presented at the age of 77 yr with a low serum cobalamin level. Subsequent study showed that he had persistently very low R binder (TC I) cobalamin-binding capacity in serum (less than 5 ng/liter versus 213 +/- 171 ng/liter in normal controls), and that almost all of his endogenous serum cobalamin was carried by TC II instead of TC I. His saliva also demonstrated virtually undetectable R binder (binding capacity of 31–38 ng/liter versus 41,690 +/- 23,820 ng/liter for control subjects). Unlike previous cases of R binder deficiency, he seemed to maintain normal serum cobalamin levels while receiving monthly cyanocobalamin injections. This and his normal serum unsaturated binding capacity were due to elevated TC II levels. TC II carried 72%-98% of his endogenous cobalamin, the rest being attached to minor binders. As incidental findings, the patient had a serum component of molecular weight of approximately 70,000 that carried 7%- 8% of his endogenous cobalamin and also had small quantities of TC II demonstrable in his saliva. Both these heretofore unappreciated minor peaks were identifiable because of the lack of R binder. The patient's clinical presentation supports the conclusion that R binder deficiency is a benign disorder. Whether his mild hypersegmentation of neutrophils and neuropathy were related to the R binder deficiency or, more likely, arose from coexisting folate deficiency and alcohol abuse, the overall picture contrasts dramatically with the severe clinical sequelae of TC II deficiency.

scholarly journals A new case of deficiency of the R binder for cobalamin, with observations on minor cobalamin-binding proteins in serum and saliva

Blood ◽  
1982 ◽  
Vol 59 (1) ◽  
pp. 152-156 ◽  
Author(s):  
R Carmel
Keyword(s):  
Molecular Weight ◽  
Alcohol Abuse ◽  
Incidental Findings ◽  
Clinical Presentation ◽  
Binding Capacity ◽  
Normal Serum ◽  
Serum Component ◽  
Almost All ◽  
Normal Controls ◽  
Low Serum

Abstract A patient presented at the age of 77 yr with a low serum cobalamin level. Subsequent study showed that he had persistently very low R binder (TC I) cobalamin-binding capacity in serum (less than 5 ng/liter versus 213 +/- 171 ng/liter in normal controls), and that almost all of his endogenous serum cobalamin was carried by TC II instead of TC I. His saliva also demonstrated virtually undetectable R binder (binding capacity of 31–38 ng/liter versus 41,690 +/- 23,820 ng/liter for control subjects). Unlike previous cases of R binder deficiency, he seemed to maintain normal serum cobalamin levels while receiving monthly cyanocobalamin injections. This and his normal serum unsaturated binding capacity were due to elevated TC II levels. TC II carried 72%-98% of his endogenous cobalamin, the rest being attached to minor binders. As incidental findings, the patient had a serum component of molecular weight of approximately 70,000 that carried 7%- 8% of his endogenous cobalamin and also had small quantities of TC II demonstrable in his saliva. Both these heretofore unappreciated minor peaks were identifiable because of the lack of R binder. The patient's clinical presentation supports the conclusion that R binder deficiency is a benign disorder. Whether his mild hypersegmentation of neutrophils and neuropathy were related to the R binder deficiency or, more likely, arose from coexisting folate deficiency and alcohol abuse, the overall picture contrasts dramatically with the severe clinical sequelae of TC II deficiency.

scholarly journals Gel Filtration Studies of Serum B12 Binding: An Abnormal Pattern in Patients with Vitamin B12 Deficiency

Blood ◽  
1969 ◽  
Vol 34 (6) ◽  
pp. 774-781 ◽  
Author(s):  
CHRISTINE LAWRENCE
Keyword(s):  
Molecular Weight ◽  
Vitamin B12 ◽  
Binding Capacity ◽  
Gel Filtration ◽  
Vitamin B12 Deficiency ◽  
Normal Serum ◽  
B12 Deficiency ◽  
Abnormal Pattern ◽  
Normal Controls

Abstract 57CoB12 was added to serum in vitro to study its binding by the three known serum B12-binders in patients with vitamin B12 deficiency and in normal controls. Gel filtration through columns of Sephadex G-200 was used to separate the low (beta) and high (alpha1 and beta) molecular weight B12-binding fractions. Electrophoresis on filter paper was used to separate the alpha1- and beta-globulins. The alpha1-globulin fraction in the serum of B12-deficient patients bound more of the added 57CoB12 than did this fraction in normal serum, presumably because this binder of the serum endogenous vitamin B12 is much less saturated in B12-deficiency. However, the total B12 binding capacity of the alpha1-globulin (for endogenous plus added vitamin B12) was lower in B12-deficient than in normal serum. The low molecular weight beta-binder bound more added 57CoB12 in B12-deficient than in normal serum, whereas the high molecular weight beta binder had a much lower B12-binding capacity in deficient than in normal serum. These abnormalities were independent of the cause of the vitamin B12 deficiency and disappeared after successful treatment with vitamin B12.

State of iron(III) in normal human serum: low molecular weight and protein ligands besides transferrin

1970 ◽  
Vol 48 (12) ◽  
pp. 1339-1350 ◽  
Author(s):  
Bibudhendra Sarkar
Keyword(s):  
Molecular Weight ◽  
Human Serum ◽  
Binding Capacity ◽  
Normal Serum ◽  
Normal Human Serum ◽  
Void Volume ◽  
Antibody Concentration ◽  
Low Molecular Weight ◽  
Protein Ligands ◽  
Normal Human

A fraction of Fe(III) in normal human serum is bound to both low molecular weight as well as protein ligands besides transferrin. Citrate was shown to be the major Fe(III)-binding substance in the low molecular weight fraction. Amino acids, sugars, and organic acids, such as ascorbate, pyruvate, and lactate, showed very little or no binding to Fe(III) in normal serum. Iron(III)-binding proteins other than transferrin were shown to be present in normal serum when the native serum with [59Fe(III)] was fractionated by (NH4)2SO4 and Sephadex G-150. The presence of these proteins was observed when trace amounts of Fe(III) were added to the normal serum and when the iron-binding capacity was saturated with Fe(III) to 50% and 100%. These proteins were eluted in the void volume of Sephadex G-150 and none of them corresponded electrophoretically to transferrin. The results of the gel filtration of a mixture of [131I]-transferrin and the proteins eluted in the void volume of Sephadex G-150 were strongly in favor of the Fe(III)-proteins as being neither transferrin aggregates nor transferrin adducts with other proteins. Immunoelectrophoresis of the Sephadex G-150 void volume proteins on agar gel against the antibody to transferrin revealed the absence of transferrin. The presence of at least six proteins in this fraction was shown by immunoelectrophoresis. Positive precipitin reactions were obtained with the antibodies to α2-macroglobulin, γG-globulin, γA-globulin, and γM-globulin. At least two more proteins in this fraction remained unidentified. When the same fraction containing [59Fe(III)] was treated with the whole antisera and the precipitates were counted for radioactivity, a typical antigen-antibody reaction curve was obtained as the antibody concentration was increased. Similar experiments with this fraction and antibodies to α2-macroglobulin, γG-globulin, γA-globulin, and γM-globulin failed to show any significant radioactivity in the precipitate. Since this fraction did not contain any transferrin, it was concluded that there are proteins besides transferrin which can act as ligands for Fe(III) in normal blood plasma.

BIOCOLLOIDS IN NORMAL HUMAN URINE: II. PHYSICOCHEMICAL AND IMMUNOCHEMICAL CHARACTERISTICS

1958 ◽  
Vol 36 (11) ◽  
pp. 1167-1175 ◽  
Author(s):  
T. Webb ◽  
B. Rose ◽  
A. H. Sehon
Keyword(s):  
Molecular Weight ◽  
Normal Serum ◽  
Low Molecular Weight ◽  
Free Diffusion ◽  
Albumin Fraction ◽  
Serum Component ◽  
Normal Human ◽  
Normal Urine ◽  
Immunochemical Characteristics ◽  
Serum Components

The biocolloids of normal urine were separated by electrophoresis on starch and compared with similarly prepared fractions of serum by ultracentrifugal, free diffusion, and immunochemical techniques. The albumin fraction of urine was indistinguishable from the serum component. The urinary γ2-globulins were shown to consist of low molecular weight (10,000) fragments of the normal serum components. The other globulins of the urine were antigenically related to some of the serum components but appeared to contain lower molecular weight materials. Some of the components of normal serum could not be detected in the urine and the urine contained at least two components which were not present in the serum.

BIOCOLLOIDS IN NORMAL HUMAN URINE: II. PHYSICOCHEMICAL AND IMMUNOCHEMICAL CHARACTERISTICS

1958 ◽  
Vol 36 (1) ◽  
pp. 1167-1175 ◽  
Author(s):  
T. Webb ◽  
B. Rose ◽  
A. H. Sehon
Keyword(s):  
Molecular Weight ◽  
Normal Serum ◽  
Low Molecular Weight ◽  
Free Diffusion ◽  
Albumin Fraction ◽  
Serum Component ◽  
Normal Human ◽  
Normal Urine ◽  
Immunochemical Characteristics ◽  
Serum Components

The biocolloids of normal urine were separated by electrophoresis on starch and compared with similarly prepared fractions of serum by ultracentrifugal, free diffusion, and immunochemical techniques. The albumin fraction of urine was indistinguishable from the serum component. The urinary γ2-globulins were shown to consist of low molecular weight (10,000) fragments of the normal serum components. The other globulins of the urine were antigenically related to some of the serum components but appeared to contain lower molecular weight materials. Some of the components of normal serum could not be detected in the urine and the urine contained at least two components which were not present in the serum.

Psychopathology in Bronchial Asthmatic Patients

1970 ◽  
Vol 15 (3) ◽  
pp. 102-107
Author(s):  
A. K. Zealley ◽  
R. C. B. Aitken ◽  
S. V. Rosenthal
Keyword(s):  
Clinical Presentation ◽  
External Resistance ◽  
Continuous Type ◽  
Asthmatic Patients ◽  
Self Confidence ◽  
Normal Ranges ◽  
Psychophysiological Examination ◽  
Pulmonary Disorder ◽  
Almost All ◽  
Normal Controls

A tripartite study of randomly selected adult asthmatics is reported, observations being by means of interview and psychometric tests and psychophysiological examination while breathing both freely and against external resistance. Results from normal and neurotic controls are compared. At interview, traits of obsessionality, dependency, sensitivity, anxiety and low self-confidence were commoner in asthmatics than normal controls. In tests of neuroticism, hostility and anxiety, asthmatics consistently lay intermediate between normals and neurotics, though their scores were almost all within the published normal ranges. Breathing against resistance, only the neurotics failed to hyperventilate: episodic asthmatics hyperventilated the most. As the patients with the more severe pulmonary disorder (asthma of continuous type) revealed less evidence of neuroticism, it was concluded that psychopathology need not be implicated as the cause of the asthmatic diathesis; it is as likely that the concomitant psychopathology only determines the clinical presentation.

Parallel Reduction of Plasma Levels of High and Low Molecular Weight Kininogen in Patients with Cirrhosis

1999 ◽  
Vol 82 (11) ◽  
pp. 1428-1432 ◽  
Author(s):  
Cheryl Scott ◽  
Francesco Salerno ◽  
Elettra Lorenzano ◽  
Werner Müller-Esterl ◽  
Angelo Agostoni ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Liver Disease ◽  
Liver Function ◽  
Plasma Levels ◽  
Plasma Concentrations ◽  
Normal Subjects ◽  
Low Molecular Weight ◽  
Major Band ◽  
Sds Page ◽  
Normal Controls

SummaryLittle is known about the regulation of high-molecular-weight-kininogen (HK) and low-molecular-weight-kininogen (LK) or the relationship of each to the degree of liver function impairment in patients with cirrhosis. In this study, we evaluated HK and LK quantitatively by a recently described particle concentration fluorescence immunoassay (PCFIA) and qualitatively by SDS PAGE and immunoblotting analyses in plasma from 33 patients with cirrhosis presenting various degrees of impairment of liver function. Thirty-three healthy subjects served as normal controls. Patients with cirrhosis had significantly lower plasma levels of HK (median 49 μg/ml [range 22-99 μg/ml]) and LK (58 μg/ml [15-100 μg/ml]) than normal subjects (HK 83 μg/ml [65-115 μg/ml]; LK 80 μg/ml [45-120 μg/ml]) (p < 0.0001). The plasma concentrations of HK and LK were directly related to plasma levels of cholinesterase (P < 0.0001) and albumin (P < 0.0001 and P < 0.001) and inversely to the Child-Pugh score (P < 0.0001) and to prothrombin time ratio (P < 0.0001) (reflecting the clinical and laboratory abnormalities in liver disease). Similar to normal individuals, in patients with cirrhosis, plasma HK and LK levels paralleled one another, suggesting that a coordinate regulation of those proteins persists in liver disease. SDS PAGE and immunoblotting analyses of kininogens in cirrhotic plasma showed a pattern similar to that observed in normal controls for LK (a single band at 66 kDa) with some lower molecular weight forms noted in cirrhotic plasma. A slight increase of cleavage of HK (a major band at 130 kDa and a faint but increased band at 107 kDa) was evident. The increased cleavage of HK was confirmed by the lower cleaved kininogen index (CKI), as compared to normal controls. These data suggest a defect in hepatic synthesis as well as increased destructive cleavage of both kininogens in plasma from patients with cirrhosis. The decrease of important regulatory proteins like kininogens may contribute to the imbalance in coagulation and fibrinolytic systems, which frequently occurs in cirrhotic patients.

Antiheparin Activity of Human Serum and Platelet Factor 4

1973 ◽  
Vol 30 (01) ◽  
pp. 093-105 ◽  
Author(s):  
C.H.J Sear ◽  
L Poller ◽  
F.R.C Path
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
Blood Serum ◽  
Whole Blood ◽  
Platelet Rich Plasma ◽  
Gel Filtration ◽  
Normal Serum ◽  
Platelet Factor ◽  
Mean Values ◽  
Antiheparin Activity

SummaryThe antiheparin activity of normal serum has been studied by comparing the antiheparin activities of sera obtained from normal whole blood, platelet-rich plasma and platelet-’free’ plasma with a purified platelet extract during differential isoelectric precipitation and by gel filtration chromatography.The mean values for the activity of PRP-serum and PFP-serum were 106% (S.D. 11) and 10% (S.D. 3) of untreated whole blood respectively. The activity of whole blood serum, PRP serum and whole blood serum plus platelet extract precipitated under identical physical conditions, i.e. pH 7.0, I =0.008, indicating that the activities of the three samples are probably associated with PF4. PF4 precipitated from human platelet extract at pH 4.0, but this is probably due to the difference in the two biochemical environments investigated, i.e. serum and platelet extract.The gel filtration experiments revealed striking similarities between the major antiheparin activities of serum and platelet extract. At physiological pH and ionic strength both activities were associated with high molecular weight material, but at physiological pH and elevated ionic strength both activities behaved as much smaller entities of molecular weight between 25,000 and 30,000 daltons and it seems very likely that both activities are associated with the same molecule, i.e. PF4.

scholarly journals Low Serum Alpha-1 Antitrypsin (AAT) in Family Members of Individuals with Autism Correlates with PiMZ Genotype

2009 ◽  
Vol 4 ◽  
pp. BMI.S1115 ◽  
Author(s):  
Anthony J. Russo ◽  
Lauren Neville ◽  
Christine Wroge
Keyword(s):  
Gastrointestinal Disease ◽  
Family Members ◽  
Serum Levels ◽  
Normal Serum ◽  
Autistic Children ◽  
Respiratory Problems ◽  
Low Levels ◽  
Alpha 1 Antitrypsin ◽  
And Gender ◽  
Low Serum

Aim Deficiency of Alpha-1-antitrypsin (AAT) can be a genetic condition that increases the risk of developing liver, lung and possibly gastrointestinal disease. Since many autistic children also have gastrointestinal disorders, this study was designed to measure serum concentration of AAT and establish AAT genotypes in autistic children, age and gender matched non-autistic siblings, parents and controls. Subjects and Methods We used an indirect ELISA with monoclonal IgG to AAT to measure AAT serum concentrations in 71 members from 16 families of individuals with autism and 18 controls (no family history of autism). We used a duplex polymerase chain reaction to detect M, S and Z alleles for alpha-1 antitrypsin expression in 52 members of 12 of the above families. Results A significantly high number of autistic family members had lower than normal serum levels of AAT when compared to controls. Autistic children with regressive onset had significantly lower levels of AAT compared to controls, and a significant number of autistic children with low serum AAT also had hyperbilirubinemia, gastrointestinal disease and respiratory problems. We also found that a significantly high number of these individuals had the PiMZ genotype and correspondingly low levels of serum alpha-1 antitrypsin. Discussion Knowing that low levels of alpha-1 antitrypsin may be inherited, and that low levels of AAT may be associated with GI disease in autistic children, genotyping autistic children may help identify individuals susceptible to developing digestive problems.

Study On Combustibility of Urethane-Modified Polyisocyanurate Foam

1983 ◽  
Vol 1 (5) ◽  
pp. 348-363 ◽  
Author(s):  
Yoshio Imai ◽  
Takao Inukai ◽  
Masato Tamashima
Keyword(s):  
Molecular Weight ◽  
Polyurethane Foams ◽  
Lower Molecular Weight ◽  
Combustion Behavior ◽  
Smoke Generation ◽  
Rigid Poly ◽  
Almost All

The relation between components of urethane-modified polyisocyanurate foams and their combustion behavior was observed to compare with rigid poly urethane foams, using the specially designed burning test apparatuses. Accord ing to the vertical smoke-weight determination for chipped samples, almost all foams lost their weight at about 650 °C. The amount of generated smoke became maximum at about 500 °C for polyurethane foams and at about 600 °C for polyisocyanurate foams. According to the horizontal smoke-concentration deter mination for small plate samples, fires occurred with much amount of generated smoke at about 600 °C. Through both the testings, adoption of higher functional isocyanate, secondary polyol, lower molecular weight polyol, or amine catalyst brought much smoke generation. Polyisocyanurate foams showed little smoke as compared with polyurethane foams.

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