PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 1799963

Buffalo thyroglobulin.

V Deshpande
View original source ↗Export metadata ↓

Abstract

1. Buffalo thyroglobulin is the major iodoprotein of buffalo thyroid with a sedimentation coefficient of 19 S and an apparent molecular mass of 685 kDa. 2. The protein is rich in iodine (1-2%) and thyroxine bound iodine (75%), unlike thyroglobulins of other mammalian species. 3. As a glycoprotein, it has the same sugar residues as noted for other thyroglobulins, and the total carbohydrate content varies from 8.41 to 9.61%. 4. Amino acid composition of buffalo thyroglobulin is similar to other species. However, the protein has 2% more proline than other mammalian thyroglobulins. 5. Glutamic acid is the sole N-terminal amino acid of buffalo thyroglobulin, in contrast to aspartic acid or asparagine for several other species. 6. The quaternary structure of the protein appears to be comprised of eight non-identical subunits.

Explore related subjects

Amino AcidsAnimalsBuffaloesCarbohydratesGlycoproteinsIodoproteinsMacromolecular SubstancesProtein ConformationThyroglobulinJournal ArticleReview

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

V Deshpande. 1991. Buffalo thyroglobulin.. https://doi.org/10.1016/0305-0491(91)90364-j

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2026

Chimeric structural isomer fragments as cost-efficient internal standards for amino acid quantification by mass spectrometry.

Amino acid (AA) profiles from body fluids such as blood and urine are clinical indicators for diagnosing metabolic and hepatic diseases. Current quantitative methods, such as liquid chromatography-mass spectrometry (LC-MS) with isotopically labelled internal standards (ISs), are costly and technically demanding. This study proposes a cost-efficient alternative using structural isomers as ISs in a direct liquid infusion (DLI) tandem mass spectrometry (MS/MS) approach. The method leverages chimeric spectra and fragment intensity ratios to quantify AAs, demonstrating high linearity and precision even with a 3D ion trap mass analyser. This approach offers a viable strategy for AA quantification in preventive medicine, particularly for screening metabolic diseases such as phenylketonuria, diabetes, and liver dysfunction.

Amino Acids↗
PubMed1992

A practical method for uniform isotopic labeling of recombinant proteins in mammalian cells.

A method to obtain uniformly isotopically labeled (15N and 15N/13C) protein from mammalian cells is described. The method involves preparation of isotopically labeled media consisting of amino acids isolated from bacterial and algal extracts supplemented with cysteine and enzymatically synthesized glutamine. The approach is demonstrated by producing 15N-labeled and 15N/13C-labeled urokinase from Sp2/0 cells and successfully growing Chinese hamster ovary (CHO) cells on the labeled media. Thus, using the procedures described, isotopically labeled proteins that have been expressed in mammalian cells can be prepared, allowing them to be studied by heteronuclear multidimensional NMR techniques.

Amino Acids↗
PubMed1992

A novel alpha-type fibrinogenase from Agkistrodon rhodostoma snake venom.

By means of CM-Sephadex C-50 column chromatography, gel-filtration on sephadex G-75 and Sephacryl S-200 columns, a purified fibrinogenase, kistomin, was obtained from venom of Agkistrodon rhodostoma. It was a single peptide-chain with a molecular mass of about 21,800 Da containing about 202 amino-acid residues as revealed by amino acid analysis. Kistomin preferentially cleaved A alpha- and subsequently the gamma-chain of fibrinogen, leaving the B beta-chain unaffected. Its fibrinogenolytic activity was estimated to be 36.6 +/- 4.5 mg/min per mg protein and was inhibited by the pretreatment of EDTA, suggesting that it is a metalloproteinase. Its fibrinogenolytic activity in platelet-poor plasma is much less potent as compared to that in purified fibrinogen solution. It inhibited ristocetin-induced aggregation of human platelets in a dose-dependent manner in the presence of von Willebrand factor.

Amino Acids↗