Preparation of cellulose with controlled molecular weight via ultrasonic treatment improves cholesterol‐binding capacity

2019 ◽  
Vol 44 (2) ◽  
Author(s):  
Ling Yan ◽  
Bing Liu ◽  
Changhong Liu ◽  
Hao Qu ◽  
Zhengzhu Zhang ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Ultrasonic Treatment ◽  
Binding Capacity ◽  
Cholesterol Binding

scholarly journals Effect of the molecular weight of water-soluble chitosan on its fat-/cholesterol-binding capacities and inhibitory activities to pancreatic lipase

PeerJ ◽  
2017 ◽  
Vol 5 ◽  
pp. e3279 ◽  
Author(s):  
Qiu Jin ◽  
Huahua Yu ◽  
Xueqin Wang ◽  
Kecheng Li ◽  
Pengcheng Li
Keyword(s):  
Molecular Weight ◽  
Pancreatic Lipase ◽  
Binding Capacity ◽  
Average Molecular Weight ◽  
Caloric Intake ◽  
Oxidative Degradation ◽  
Water Soluble ◽  
Treatment And Prevention ◽  
Cholesterol Binding

BackgroundObesity has become a worldwide burden to public health in recent decades. Given that obesity is caused by an imbalance between caloric intake and expenditure, and that dietary fat is the most important energy source of all macronutrients (by providing the most calories), a valuable strategy for obesity treatment and prevention is to block fat absorption via the gastrointestinal pathway. In this study, the fat- and cholesterol-binding capacities and the inhibition of pancreatic lipase by water-soluble chitosan (WSC) with different weight-average molecular weight (Mw) were tested and comparedin vitro, in order to determine the anti-obesity effects of WSC and the influence of its Mw.MethodsIn this study, WSC with different Mw (∼1,000, ∼3,000, ∼5,000, ∼7,000 and ∼9,000 Da) were prepared by oxidative degradation assisted with microwave irradiation. A biopharmaceutical model of the digestive tract was used to determine the fat- and cholesterol-binding capacity of WSC samples. The pancreatic lipase assays were based on p-nitrophenyl derivatives.ResultsThe results showed that all of the WSC samples exhibit great fat- and cholesterol-binding capacities. Within the testing range, 1 g of WSC sample could absorb 2–8 g of peanut oil or 50–65 mg of cholesterol, which are both significantly higher than the ability of cellulose to do the same. Meanwhile, all the WSC samples were proven to be able to inhibit pancreatic lipase activity to some extent.DiscussionBased on the results, we suggest that there is a significant correlation between the binding capacity of WSC and its Mw, as WSC2 (∼3,000 Da) shows the highest fat- and cholesterol-binding capacities (7.08 g g−1and 63.48 mg g−1, respectively), and the binding ability of WSC declines as its Mw increases or decreases from 3,000 Da. We also suggest WSC as an excellent resource in the development of functional foods against obesity for its adsorption, electrostatic binding and entrapment of cholesterol, fat, sterols and triglycerides in the diet.

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.

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.

STUDIES ON SMALL MOLECULAR WEIGHT ADHESION PROTEINS (SAPs) FROM CONNECTIVE TISSUES

1987 ◽  
Author(s):  
S Wasi ◽  
P Alles ◽  
D Gauthier ◽  
U Bhargava ◽  
J Farsi ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Polyclonal Antibody ◽  
Type I Collagen ◽  
Cell Attachment ◽  
Binding Capacity ◽  
Guanidine Hydrochloride ◽  
Cell Types ◽  
Type I ◽  
Cell Binding ◽  
Connective Tissues

We have identified a family of low molecular weight proteins with cell attachment properties in a variety of soft and mineralised connective tissues (Wong et al., Biochem. J. 232, 119, 1985). For further characterisation of these proteins we extracted porcine bones with 4 M guanidine hydrochloride and purified the proteins on a series of gel filtration columns The purifed SAPs comprise three bands with Mr -14 000 -17 000. All three proteins bound to heparin-sepahrose in both the presence and absence of 4M urea, and when eluted with 2 M NaCl they retained their cell binding capacity. These proteins promoted the adhesion and spreading of a variety of cell types, including normal fibroblasts, osteoblasts, and epithelial cells, and tumour (osteosarcoma) cells. On Western blotting SAPs did not cross-react with antibodies against fibronectin, laminin or type I collagen; however, they were recognised by a monoclonal antibody to human vitronectin, a polyclonal antibody to bovine vitronectin and polyclonal antibody to human somatomedin B. Dose response experiments indicated that maximum attachment of human gingival fibroblasts occurred in the presence or absence of fetal bovine serum on wells precoated with 2.5 μg/cm2 of SAPs. Attachment of cells to these proteins was partially inhibited by the synthetic pentapeptide Gly-Arg-Gly-Asp-Ser. Utilising the nitrocellulose cell binding assay of Hayman et al (J. Cell. Biol. 95, 20, 1982), the cell attachment to these proteins could be completely inhibited by heparin (100 units/mL) whereas up to 1000 units/mL of heparin had no inhibitory effect on cell attachment to fibronectin and vitronectin. The occurrence of these proteins in a variety of connective tissues and their recognition by different cell types may reflect their general biological role in adhesive mechanisms in both hard and soft connective tissues. Currently, we are investigating the relationship between SAPs and vitronectin, since it is possible that SAPs represent a tissue-processed form of vitronectin or may be novel attachment proteins with regions of homology with vitronectin

Lead-binding capacity of calcium pectates with different molecular weight

2017 ◽  
Vol 97 ◽  
pp. 526-535 ◽  
Author(s):  
Maksim Khotimchenko ◽  
Ksenia Makarova ◽  
Elena Khozhaenko ◽  
Valeri Kovalev
Keyword(s):  
Molecular Weight ◽  
Binding Capacity ◽  
Different Molecular Weight

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.

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