Antinociceptive activities of Asn-Ala-Gly-Ala and its analogue in mice.

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود 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

N-Ac-Ser-Asn-Lys-Phe-Leu-Gly-Thr- Trp-Lys-Leu-Val-Ser-Ser-Glu-Asn-Phe-Asp-Asp-Tyr- Met-Lys-Ala-Leu-Gly-Val-Gly-Leu-Ala-Thr-Arg-Lys- Leu-Gly-Asn-Leu-Ala-Lys-Pro-Asn-Val-Ile-Ile-Ser- Lys-Lys-Gly-Asp-Ile-Ile-Thr-Ile-Arg-Thr-Glu-Ser-Gly-

The reaction of the P2 protein from rabbit sciatic nerve with CNBr produced four peptides: a 20-residue peptide (CN3) containing tryptophan which occupies the blocked NHZ terminus; Peptide CN1, a large peptide comprising over 70% of the P2 molecule; Peptide CN2, a fraction containing two tightly bound peptides having 2 half-cystine residues and comprising the COOH terminus; and Peptide CN4, a n...

متن کامل

N-Ac-Ser-Asn-Lys-Phe-Leu-Gly-Thr- Trp-Lys-Leu-Val-Ser-Ser-Glu-Asn-Phe-Asp-Asp-Tyr- Met-Lys-Ala-Leu-Gly-Val-Gly-Leu-Ala-Thr-Arg-Lys- Leu-Gly-Asn-Leu-Ala-Lys-Pro-Asn-Val-Ile-Ile-Ser-

The reaction of the P2 protein from rabbit sciatic nerve with CNBr produced four peptides: a 20-residue peptide (CN3) containing tryptophan which occupies the blocked NHZ terminus; Peptide CN1, a large peptide comprising over 70% of the P2 molecule; Peptide CN2, a fraction containing two tightly bound peptides having 2 half-cystine residues and comprising the COOH terminus; and Peptide CN4, a n...

متن کامل

Differences between β-Ala and Gly-Gly in the design of amino acids-based hydrogels

Despite the continuous interest in organogels and hydrogels of low molecular weight gelators (LMWG), establishing the relationship between the molecular structure and the gelation mechanism is still a challenge. In this paper our interest focuses on the consequences of slight molecular modifications on the self-assembling behaviour of β-Ala vs Gly-Gly-based hydrogelators. Previously, in our gro...

متن کامل

Pressure Dependence of 15N Chemical Shifts in Model Peptides Ac-Gly-Gly-X-Ala-NH2

High pressure NMR spectroscopy has developed into an important tool for studying conformational equilibria of proteins in solution. We have studied the amide proton and nitrogen chemical shifts of the 20 canonical amino acids X in the random-coil model peptide Ac-Gly-Gly-X-Ala-NH2, in a pressure range from 0.1 to 200 MPa, at a proton resonance frequency of 800 MHz. The obtained data allowed the...

متن کامل

Oligopeptides with the sequences ala-pro-gly and gly-pro-gly as substrates or inhibitors for protocollagen proline hydroxylase.

Sequential oligopeptides prepared by condensation of peptides with the sequence Ala-Pro-Gly or Gly-Pro-Gly were examined as possible substrates or inhibitors for the synthesis of hydroxyproline by protocollagen proline hydroxylase. The tripeptide BOC-Ala-Pro-Gly-OMe (where BOC-represents 1-butoxycarboxyland Me represents methyl) was not hydroxylated, but oligopeptides ranging in size from BOC(A...

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: Japanese Journal of Pharmacology

سال: 1985

ISSN: 0021-5198

DOI: 10.1016/s0021-5198(19)63657-7