The effects of angiogenesis inhibitor from the extract libraries of Korean and Chinese medicinal plants were investigated using a protein microarray chip. Protein chip was constructed by immobilization of integrin α5β1 on protein chip base plates and employed far screening active extracts that inhibit the integrin-fibronectin interaction from the extract libraries. The 100 extracts of medicinal plants were obtained from extract bank of National Institute of Crop Science, RDA. The 14 extracts among 100 extract libraries were shown efficient inhibition activity for the interaction between integrin-fibronectin. The medicinal plants of 14 extracts were Vitex negundo var. incisa (Lam.) C.B. Clarke, Epimedium koreanum Nakai, Cedrela sinensis A. Juss, Ipomea aquatica Forsk, Schisandra chinensis Baill, Pulsatilla koreana Nakai, Paeonia lactiflora Pall. var.hortensis Makino, Oenothera odorata, Allium chinense, Allium victorialis var. platyphyllum MAKINO, Polygonatum odoratum Druce var. pluriflorum Ohwi, Hosta lancifolia, Agrimonia pilosa L. var. japonica Nakai and Potentilla chinensis SER. The Paeonia lactiflora, Oenothera, and Agrimonia pilosa from these 14 extracts libraries were shown strong inhibition activity of integrin α5β1.

광계II(PSII)는 고등식물의 chloroplast에서 두 개의 광합성 반응중심 중의 하나이다. Chlorophyll a/b 광수확 복합체는 광계II를 위한 안테나 역할을 수행한다. 본 연구에서는 인삼의 잎조직을 제작한 cDNA library로부터 chlorophyll a/b-binding protein (Cab) 유전자를 분리하였다. 인삼 Cab유전자는 935 bp의 염기와 265개의 아미노산 잔기(pI 5.63)로 구성된 한 개의 ORF를 포함하고 있으며, 단백질의 분자량은 28.6 kDa으로 추정되었다. 인삼에서 분리한 Cab 유전자는 기존에 식물에서 보고된 유전자들과 유사성을 나타내었으며, 유사도는 68-92%로 나타났다. 아미노산 서열을 비교하여 유연관계를 분석한 결과 인삼의 Cab 유전자는 비교된 P. persica (AAC34983), A.thaliana (AAD28771), G. hirsutum (CAA38025), G. max (AAL29886), V. radiata (AAF89205) 등과 동일한 그룹으로 분리되었다.

This study was carried out to investigate the functional properties such as nitrogen solubility, emulsifying property , foaming capapcity , water and oil absorption of Camellia (Camellia japonica .) seed protein isolate in condition of distilled water and 0.5M NaCl solution at pH 2.0∼10.0. Nitrogen solubility of Camellia protein isolate in distilled water showed the minimum value at pH 4.0 and increased at pH lower or higher than the isoelectric point(pH 4.0). It was 90.0 %at pH 10.0 Nitrogen solubility of 0.5M NaCl solution showed a similar pattern with that of distrille dwater but was higher than that of distilled water except pH 2.0 and pH 10.0. Emulsifying activity of Camellia seed protein islate showed the minimum value at pH 4.0, but was higher at ether value of pH. Emulsifying stability of protein isolate was stable by heat treatment for 30min, at 80℃ and increased in 0.5M NaCl solution more than that of distille dwater. Foaming capacity of Camellia seed protein isolate in distill3ed water showed the minimum value near the isoelectric point, While it changed little at other values of pH. Foaming stability slowly decreased as, but didn't make a significant difference as time was delayed . Oil absorption was 1.4ml per a sample of 1g and water absorption was 0.9ml per a sample of 1g. The former was higher than the latter . The content of total amino acid of Camellia protein isolate was 43.67% and the major total amino acid of Camellia protein isolate was 43.67% and the major total amino acid was in the order of glutamic acid , arginine, aspartic acid, and leucine.

A cDNA Fragment encoding iron storage protrin generated by polymerase chain reaction(PCR) using highly conserved regions of ferritin related genes were used to sereen a red pepper cDNA library. cDNA clone was designated as Fp1. Fp1 clone contatines a 5' nontranslated region of 51dp containing stop conds. Down stream from 5' UTP. an open reading frame of 750bp was observed. followed by a 3' UTR of 272bp. The deduces amino acid sequence of red pepper protein(Fp1) showed 84%, 48% and 36% identity with soybean(SolC). human(HuL H) and horse spleen(HoS-L) ferritin mRNA accumulation in response to iron. Ferritin mRNA accumulation was transient and particularly abundant in leaves. reaching a maxmum at 12h. The level of ferritin mRNA in roots was affected to a lesser extent than in leaves.