Purification and Properties of Blood-Group-Specific Lectins from Vicia cracca
نویسندگان
چکیده
منابع مشابه
Isozyme variation and phylogenetic relationships in Vicia subgenus Cracca (Fabaceae).
BACKGROUND AND AIMS The phylogenetic relationships among 27 vetch species belonging to the subgenus Cracca of the genus Vicia were studied in comparison with three species of Lathyrus section Lathyrus on the basis of isozyme variation. METHODS Isozymes encoded by 15 putative loci of ten enzymes were resolved by polyacrylamide gel electrophoresis and isozyme variation was analysed by using par...
متن کاملextraction and acetylation of purified trypsin from bovin pancreas and study of some its physico-chemical properties
آنزیم تریپسین در شرایط قلیایی ناپایدار می باشد .و فعالیت پروتئولیتیکی تریپسین منجربه خود هضمی آن در جایگاههای خاصی می گردد. بنابر این آنزیمی با ناپایداری بالا محسوب میگردد. در سالهای اخیر موفق شدند که با ایجاد تغیرات شیمیایی با اضافه کردن فلزات خاص ، کلسیم و یا عمل استیلاسیون منجر به افزایش پایداری آنزیم تریپسین گردند. مطالعات در حال حاضر نشان می دهد که تریپسین استیله شده فعالیت آنزیمی خود را ...
15 صفحه اولsialic acid specific lectins from episesarma tetragonum (decapoda, grapsidae): isolation, purification and characterization
two sialic acid specific lectins episesarma tetragonum agglutinin–1 and 2 were purified from the hemolymph of the mangrove crab, episesarma tetragonum . the major lectin was purified using cnbr-activated sepharose 4b conjugated to fetuin. n-acetyl glucosamine containing buffer was used for elution. the hemagglutination activity of purified lectin was inhibited by glycoproteins containing siaα, ...
متن کاملThe Lectins of Sophora japonica: II. Purification, Properties, and N-Terminal Amino Acid Sequences of Five Lectins from Bark.
Five N-acetyl-galactosamine-specific lectins were isolated from the bark of the legume tree Sophora japonica. These lectins are immunologically and structurally very similar, but not identical, to the Sophora seed and leaf lectins. The carbohydrate specificities and hemagglutinin activities of these lectins are indistinguishable at pH 8.5 but their activities differ markedly at pH values below ...
متن کاملThe Lectins of Sophora japonica: I. Purification Properties and N-Terminal Amino Acid Sequences of Two Lectins from Leaves.
Two lectins, Leaf Lectin I and Leaf Lectin II (LLI and LLII) were purified from the leaves of Sophora japonica. Like the Sophora seed lectin, LLI and LLII are tetrameric glycoproteins containing a single subunit with respect to size. The subunits of LLI (32 kilodaltons) and LLII (34 kilodaltons) are slightly larger than those of the seed lectin (29.5 kilodaltons). The three Sophora lectins disp...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1977
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1977.tb11255.x