Human migration inhibitory factor: purification and immunochemical characterization.

نویسندگان
چکیده

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Human migration inhibitory factor: purification and immunochemical characterization

Using gel filtration and preparative isotachophoresis, the migration inhibitory factor (MIF) was highly purified from human lymphocytes activated with concanavalin A. MIF is an acidic protein with a mol wt of approximately equal to 25,000 daltons as determined by gel filtration and analytical polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The protein inhibits migr...

متن کامل

Human Migration Inhibitory Factor: Purification and Immunochemical Characterization by Lutz H. Block,* Herbert Jaksche, Stephan Bamberger, and Gerhard

Products of activated lymphocytes are known to modulate the function of macrophages (1-3). Migration inhibitory factor (MIF) 1 is one of the best studied mediators of cellular immunity (4). Although many investigators have tried to analyze the biological and physicochemical properties of MIF from different species, the active substance has not been purified to homogeneity. MIF produced by guine...

متن کامل

Purification, characterization and immunochemical detection

A phospholipase A2 (PLA2, EC 3.1.1.4) was purified from human cell-free ascitic fluid (a-PLA2) by ion-exchange chromatography and h.p.l.c. on a reverse-phase column to apparent homogeneity. The enzyme had an Mr of approx. 10000 as determined by SDS/PAGE. Polyclonal antibodies raised in a rabbit were specific to a-PLA2, as judged by immunoblotting. A time-resolved fluoroimmunoassay (TR-FIA) for ...

متن کامل

Human liver alpha-L-fucosidase. Purification, characterization, and immunochemical studies.

Human liver alpha-L-fucosidase has been purified 6300-fold to apparent homogeneity with 66% yield by a two-step affinity chromatographic procedure utilizing agarose epsilon-aminocaproyl-fucosamine. Isoelectric focusing revealed that all six isoelectric forms of the enzyme were purified. Polyacrylamide gel electrophoresis of the purified alpha-L-fucosidase demonstrated the presence of six bands ...

متن کامل

Cottonseed malate synthase : purification and immunochemical characterization.

Malate synthase (EC 4.1.3.2), an enzyme unique to the glyoxylate cycle, was purified to homogeneity from cotyledons of 72-hours, darkgrown cotton (Gossypium hirsutum L.) seedlings. Homogeneity of the enzyme was assessed by silver staining SDS-PAGE gels. Purification was accomplished by using a single buffer medium through six steps involving one ammonium sulfate fractionation and chromatography...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Journal of Experimental Medicine

سال: 1978

ISSN: 0022-1007,1540-9538

DOI: 10.1084/jem.147.2.541