Studies on the active center of human plasmin. Partial amino acid sequence of a peptide containing the active center serine residue.

نویسندگان

  • W R Groskopf
  • L Summaria
  • K C Robbins
چکیده

Tryptic digestion of the diisopropyl phosphoryl-32P-Scarboxymethyl light chain derivative of human plasmin followed by gel filtration on Sephadex G-75 and G-25 and chromatography on Dowex SOW-X2 has resulted in the isolation of three radioactive peptides. These three peptides, having 31,33, and 34 residues, are all derived from the same segment of the plasmin molecule. Structural determinations have yielded the partial amino acid sequence, Val-Glx-(Ser-Thr, Glx)-Leu-(Gly, Ala)-His-Leu-Ala-CysAsn-(Thr, Gly, Gly)-Ser-Cys-Gln-Gly-Asp-Ser(diisopropy1 phosphoryl-32P)-Gly-Gly-Pro-Leu-Val-Cys-Phe-Glu-LysAsp-Lys-Tyr.

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

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Ab Initio Quantum Chemical Studies of 15N and 13C NMR Shielding Tensors in Serine and Complexes of Serine- nH2O: Investigation on Strength of the CαH…O Hydrogen bonding in the Amino Acid Residue.

In this paper, the hydrogen bonding (HB) effects on the NMR chemical shifts of selected atoms in serineand serine-nH2O complexes (from one to ten water molecules) have been investigated with quantummechanical calculations of the 15N and 13C tensors. Interaction with water molecules causes importantchanges in geometry and electronic structure of serine.For the compound studied, the most importan...

متن کامل

Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity

Recently, antimicrobial peptides have been introduced as potent antibiotics with a wide rangeof antimicrobial activities. They have also exhibited other biological activities, including antiinflammatory,growth stimulating, and anti-cancer activities. In this study, an analog of MagaininII was designed and produced as a recombinant fusion protein. The designed sequence containe...

متن کامل

Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity

Recently, antimicrobial peptides have been introduced as potent antibiotics with a wide rangeof antimicrobial activities. They have also exhibited other biological activities, including antiinflammatory,growth stimulating, and anti-cancer activities. In this study, an analog of MagaininII was designed and produced as a recombinant fusion protein. The designed sequence containe...

متن کامل

Investigation of Consecutive Separating Arrangements of Bio active Compounds from Black Tea (Camellia sinensis) Residue

Every year lots of black tea (Camellia sinensis (L.) Kuntze) residue will produce in the factories. These residue are unusable whereas the bio active compounds can be extracted and used in the drag and food industries. Due to mentioned problems, this project was conducted years 2011 - 2012 with the aim to make a study on consecutive isolation of all bio active compounds from tea residu...

متن کامل

Identification of a glutamic acid at the active center of bovine carboxypeptidase B.

The glutamic acid residue at the active center of bovine carboxypeptidase B was labeled with a-N-bromoacetyl-D[5J4C]arginine and the alkylated protein was hydrolyzed with pepsin. A 14C-labeled peptide fraction was isolated in a 52% yield by gel filtration on Sephadex G-25 followed by ion exchange chromatography on CM-cellulose. Compositional and end group analysis, in addition to enzymatic hydr...

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

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 244 13  شماره 

صفحات  -

تاریخ انتشار 1969