type I collagen

type I col·la·gen

the most abundant collagen, which forms large well-organized fibrils having high tensile strength.

References in periodicals archive ?

These results that identify collagen from a waste source such as fish processing by-products have also been reported by Nagai and Suzuki (1999) who revealed that type I collagen could be isolated from fish skin bones and fins.

ISOLATION AND CHARACTERISATION OF COLLAGEN FROM THE WASTE MATERIAL OF TWO IMPORTNT FRESHWATER FISH SPECIES

Of note, the thermal stability of soluble type I collagen extracted by limited pepsin digestion from DD palmar tissue was higher than that of normal aponeuroses, as shown by circular dichroism measurements.

Changes of Biochemical and Biomechanical Properties in Dupuytren Disease

Type I collagen gel induces Madin-Darby canine kidney cells to become fusiform in shape and lose apicalbasal polarity.

The developmental role of the extracellular matrix suggests a monophyletic origin of the kingdom Animalia

The carboxy-terminal telopeptide of type I collagen (ICTP) cross-links with the COL domain of type I collagen in collagen matrix formation (10).

Time-dependent changes of serum carboxy-terminal peptide of type I procollagen and carboxy-terminal telopeptide of type I collagen concentrations in patients with acute myocardial infarction after successful reperfusion: correlation with left ventricular volume indices

In individual children, this may coincide with the degradation of type I collagen occurring at the same time (releasing ICTP into the circulation), either as part of the normal saltatory growth pattern [25] or during subclinical infections that may affect short-term growth [26].

Serum concentrations of carboxyl-terminal propeptide of type I procollagen, amino-terminal propeptide of type III procollagen, cross-linked carboxyl-terminal telopeptide of type I collagen, and their interrelationships in schoolchildren

Now, these rights have been expanded to include the use of regular, non-crosslinked, synthetic peptides mimicking amino acid sequences of the N-telopeptides of type I collagen, i.

Osteometer BioTech A/S Announces Allowance of European Patent for Using Synthetic Peptides to Detect N-Telopeptides of Type I Collagen, i.e. the NTX Peptide Fragments

Initially, FibroGen is offering two of the 20 known human collagens through its web site: type I collagen and type III collagen.

FibroGen Presents the Advantages of Synthetic Collagens and Gelatin at World BioMaterials Conference

Osteomark(R) is a urinary assay that provides a quantitative measure of the excretion of cross-linked N-telopeptides of type I collagen (NTx), the manufacturing and commercializing rights of which are obtained under a license from Ostex International, Inc.

Ostex International Announces Osteomark Receives Expanded Screening and Monitoring Claims in Japan

Cohesion Technologies (NASDAQ NM: CSON) today announced that the Company has demonstrated feasibility with its recombinant collagen technologies, having generated a thermally stable human Type I collagen and gelatin in yeast in a novel and proprietary form.

Cohesion Technologies Demonstrates Feasibility With Recombinant Collagen Technologies

1988-509161, includes 11 claims directed to assay methods, antibodies, and test kits for measuring N-telopeptides of type I collagen (NTx) as an indication of human bone resorption.

Japanese Patent Office Allows Two Patent Applications Protecting Ostex' Osteomark NTx Assay

5,455,179, covers a method of analyzing a body fluid sample for a type I collagen analyte (CTx) indicative of degradation of type I collagen in vivo.

Ostex International initiates patent lawsuit to protect its Osteomark technology in United States

This in vitro study reported a positive reaction of an N-telopeptides assay with skin collagen, indicating that the assay reacts generally with other type I collagen rather than being specific for bone collagen.

Metra Biosystems' Pyrilinks bone metabolism tests reported most specific in comparative research study