• BMB Reports
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• 제33권4호
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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.

• BMB Reports
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• 제40권6호
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• pp.959-965
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• 2007

Two isolectins (KML-IIU and the KML-IIL) were individually isolated from the previously reported Korean mistletoe lectin, KML-C, by using an immunoaffinity column. Molecular weights of the KML-IIU and the KML-IIL were 64 kDa and 60 kDa respectively. Both of the lectins were composed of heterogeneous A and B subunits linked with a disulfide bond, and showed the same carbohydrate-binding specificities for Gal and GalNAc. However, they are different not only in biophysical properties (glycosylation and amino acid compositions) but also bioactivities (cell killing and cytokine induction). The KML-IIL showed 17-145 times stronger in cytotoxicities to various human and mouse cancer cell lines than the KML-IIU. The KML-IIL also induced TNF-$\alpha$ secretion from mouse peritoneal macrophages 4.5 times better than the KML-IIU. The results demonstrated isolectins in Korean mistletoe were varied in bioactivities and the KML-IIL may be developed as an anti-cancer agent.

• 약학회지
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• 제39권3호
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• pp.252-259
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• 1995

Isolation, purification and characterization of biophysicochemical properties of the three new lectins, MLA-I, MLA-II, MLA-III from the hemolymph of Meretrix lusoria have been reported previously. A series of immunochemical studies were investigated in this work. The three lectins were revealed as having partial identity each other by immunodiffusim and immunoelectrophoresis. These results suggest that MLA lectins are isolectins having similar biophysicochemical properties. Particularly, MLA-I proved to be a potent mitogen for murine splenic as well as human peripheral lymphocytes, and the optimum mitogenic dose were 62.5 and 1.95 $\mu\textrm{g}$/ml, respectively.

• 한국식품영양과학회지
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• 제23권2호
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• pp.308-314
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• 1994

토란에서 정제한 lectin은 적혈구 응집활성이 서로 다른 4개의 획분 (Isolectin I, II, III, IV)으로 이루어진 당단백질로서, disk 전기영동 및 densitometric pattern 상에서 I, IV는 단일한 subunit의 단백질로서, 그리고 II, III는 I, IV는 단일한 subunit의 단백질로서, 그리고 I, II는 I, IV의 fabric 단백질로서 추정되었다. 그러나, 요소 함유 disk 전기영동에서는 I은 단일의, IV는 2종류의 subunit에서, II, III은 I, IV의 subunit에서 구성된 단백질임을 알앗다. 그래서 염소함유 초점전기영동에서도 isolectin IV는 2개의 peack가 될 것이라고 예상하였으나 실제로는 1개의 peak만이 나타났다. 또한 정제 lectin은 당, 가열, pH, 변성제, 금속에 대한 적혈구 응집저해는 거의 보이지 않았으나, pepsin에 의한 부분적인 활성 변화가 관찰되었다.

• KSBB Journal
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• 제9권2호
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• pp.115-121
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• 1994

240ml의 시료를 정제할 수 있는 30channel의 preparative-scale 자유유동전기이동 분리장치를 제작한 후 렌즈콩으로부터 lentil lectin(LcH)을 전기 집속법으로 분리하였다. 분리된 각 분획을 PAGIEF젤에서 silver staining했을 때 불순물이 전혀 검출되지 않을 정도의 고순도 lectin을 얻을 수 있었다. 이 때 ampholyte로서 HEPES(50mM) -Tris(50mM) -urea(3M) 등을 사용하였으며 50mM Histidine(pI 7.65)인 경우 가장 분리도가 가장 좋았다. LcH는 보통의 조건하에서 LcH-A와 LcH-B의 두가지 순수한 형태로만 나타났으며 따라서 이 장치를 사용하여 다단 분리 정제를 할경우 두 성분의 완전한 분리도 가능함을 보여 주었다.