• Title/Summary/Keyword: Glycoproteins

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Structural Effects of Sulfated-Glycoproteins from Stichopus japonicus on the Nitric Oxide Secretion Ability of RAW 264.7 Cells

  • Cao, Rong-An;Lee, Su-Han;You, SangGuan
    • Preventive Nutrition and Food Science
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    • v.19 no.4
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    • pp.307-313
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    • 2014
  • The effect of various levels of proteins, sulfates, and molecular weight ($M_w$) of a sulfated-glycoprotein ($NF_3$) from a sea cucumber, Stichopus japonicus, on nitric oxide (NO) releasing capacity from RAW 264.7 cells was investigated. The $NF_3$ derivatives had various amounts of proteins (4.8~11.2%) and sulfates (6.8~25.2%) as well as different $M_w$ ($640.3{\times}10^3{\sim}109.2{\times}10^3g/mol$). $NF_3$ was able to stimulate RAW 264.7 cells to release NO with lower protein contents, indicating that the protein moiety was not an important factor to stimulate macrophages. On the other hand, the NO inducing capacity was significantly reduced with decreased levels of sulfates and $M_w$, implying that sulfates and $M_w$ played a pivotal role in activating RAW 264.7 cells. It was not clear why sulfates and a certain range of $M_w$ were essential for stimulating macrophages. It appeared that certain levels of sulfates and $M_w$ of sulfated-glycoproteins were required to bind to the surface receptors on RAW 264.7 cells.

THE EFFECT OF ADHESIVE GLYCOPROTEIN ON THE ACTIVITY OF HUMAN PULP FIBROBLAST (교원질과 당단백이 치수섬유모세포에 미치는 효과에 관한 연구)

  • Kim, Ju-Yon;Choi, Ho-Young
    • Restorative Dentistry and Endodontics
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    • v.21 no.2
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    • pp.546-558
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    • 1996
  • The purpose of this vitro study was to evaluate the activity of human pulpal cells to adhesive glycoprotein-coated and non-coated culture dishes. Well known adhesive glycoproteins were used, such as type I collagen, type IV collagen, fibronectin, laminin, and vitronectin. Each adhesive glycoproteins applied onto the culture dishes. In this study, the protein coated and non-coated dishes were classified as each groups. Human pulpal cells cultured onto each groups. After 24 hours, 48 hours, 72 hours incubation time, radioactivity with scintillation counter for evaluation of the activity of human pulpal cells. The results as follows : 1. After 24 hours incubation time, activity of human pulpal cells were best in laminin-coated group among groups. Then fibronectin, type I collagen group were better, and all proteins were better than control. 2. After 48 hours incubation time, activity of human pulpal cells were best in fibronectin coated group. 3. After 72 hours incubation time, activity of human pulpal cells were not significantly different in all of adhesive glycoproteins. 4. After 24 hours incubation time, activity of human pulpal cells were best in fibronectin and laminin coated group. Activity of human pulpal cells in type I collagen coated group were better after 24 hours incubation time then 48 hours incubation time.

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Purification and Characterization of Two Isolectins with Arginase Activity from the Lichen Xanthoria parietina

  • Molina, M. C.;Vicente, C.
    • BMB Reports
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    • v.33 no.4
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    • pp.300-307
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    • 2000
  • Two glycoproteins were purified and biochemically characterized from the lichen X. parietina. Both behaved as enzymes with arginase activity and haemaglutinins. Secreted arginase (SA) contained galactose and glucose in the saccharide moiety and an isoelectric point of 4.54. The algal binding-protein (ABP) had N-acetyl-glucosamine and glucose as glycosidic residues and an isoelectric point of 3.53. Both proteins had the same molecular mass (58.6 kDa) and the same qualitative amino acidic composition. The results allowed us to consider these glycoproteins as isolectins, which have significant physiological roles in the relationship between photobiont and mycobiont of symbiotic association.

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Structure and Function of Glycoproteins in Human Saliva (인체 타액내 당단백질의 구조와 기능)

  • Song Han
    • Journal of Oral Medicine and Pain
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    • v.20 no.1
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    • pp.19-28
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    • 1995
  • 타액은 구강 환경을 조절하는 여러 가지 유기질과 무기질의 혼합물로 구성되어 있다. 구강 점막은 여러 타액 점액 단백질과 타액 항세균 단백질에 의해서 윤활이 되며 보호된다.타액의 다른 작용은 구강 점막을 축축하게 하고 음식을 부드럽게 한다. 구강건조증은 세균의 침착을 야기시키거나 점막면을 거칠게 하여 출혈이 되기 쉽게 하며 이로 인해 감염이 야기될 수 있다. 이러한 타액의 보호 작용은 mucin, fibronectins, proline-rich glycoproteins, histidine-rich proteins, $\alpha$-amylase, s-IgA 같은 특별한 타액 당단백질에 기인한다고 하는 것이 지난 30년 동안에 알려져 있다. 이러한 분자들의 구조, 구조와 기능사이의 관계, 타액 내 이러한 물질들의 농도에 관한 것들이 알려지고 있는 중이다. 이러한 타액 당단백질 특히 mucin, fibronectin, fucose-rich protein과 s-IgA의 구조와 기능에 대한 현재의 견해들을 이 논문에서 요약하고자 한다.

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Antitumor Effects of Glycoportein Extracted from Sea Cucumber (Stichopus japonicus)

  • Moon, Jeung-Hye;Ryu, Hong-Sool;Suh, Jae-Soo
    • Preventive Nutrition and Food Science
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    • v.4 no.2
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    • pp.117-121
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    • 1999
  • The anititumor and immunologic activities of the glycoproteins extracted from sea cucumber (Stichopus japonicus) on mice bearing sarcoma 180 cells were investigated . Maximum tumor suppression (64%) occurred at the dose of 100mg glycoprotein/kg. The highest prolongation ratio was achieved at the level of 100mg/kg an dincreased by 395 more than that of control. Glycoproteins from sea cucumber exhibited direct cytotoxic effect on the tumor cells. Dose dependent increase of leucocyte, peritoneal exudate cell and weights of immunoorgans revealed the improvement of immunity. When the glycoportein-administered group was compared with the control, a significant difference was not noted in the clinico-chemical values such as S-GOT, S-GPT , alkaline phoshatse activity, total protein, cholesterol, triglyceride, urea nitrogen and glucose levels in blood. These results suggests that the antitumor activity of sea cucumber glycoprotein is associated with activation of cells in the immune system.

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Purification of $\alpha$-Amylase Inhibitor from Naked Barley in Korea (한국산 쌀보리 $\alpha$-Amylase 저해물질의 분리 및 정제)

  • 심기환;문주석;신창식;최진상;박석규
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.24 no.4
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    • pp.556-562
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    • 1995
  • The $\alpha$-amylase inhibitor from naked barley was purified by DEAE-cellulose, Concanavalin-A sepharose and superose 6 column chromatography, and confirmed by capillary electrophoresis. The purified $\alpha$-amylase inhibitor showed a single band of 29KD in molecular weight when estimated by the SDS-PAGE. Its purity was increased by 12-fold as compared to its crude extract, and its specific activity was found to be 336.7units/mg. The major amino acids of the $\alpha$-amylase inhibitor from naked barley was appeared to be glutamic acid, asparitic acid and arginine. The inhibitor from naked barley was glycoproteins and carbohydrate content of inhibitor was 1.0%.

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