Binding of Mucopolysaccharides and Dyes by Collagen

Einbinder, Julia M.; Schubert, Maxwell

doi:10.1016/s0021-9258(18)56175-5

Cited by 107 publications

(5 citation statements)

References 10 publications

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“…The procedure of Mandl et al (1953) was employed except that 0.02 M Tris-HCl, pH 8.4, buffer containing 0.001 M CaCl2 was used in place of phosphate buffer, and soluble peptides released by the action of collagenases were measured by the method of Rosen (1957). Native bovine Achilles' tendon collagen used in this procedure was either a commercial preparation from Worthington Biochemical Corp. or a laboratory preparation (Einbinder & Schubert, 1951). Boiled enzyme controls were used as blanks.…”

Section: Methodsmentioning

confidence: 99%

Purification and characterization of a marine bacterial collagenase

Merkel¹,

Dreisbach²

1978

Biochemistry

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A true collagenase was isolated from the culture fluid of a marine bacterium which has been designated Vibrio B-30 (ATCC 21250). Collagenase production was obtained only in media containing collagen or certain degradation products of collagen. Partial purification on DEAE-cellulose and Sephadex G-200 columns produced active enzyme which was free of nonspecific proteases but which contained two collagenases. The two collagenases have the same apparent molecular size, and evidence is presented to support the theory that one collagenase is derived from the other. Vibrio B-30 collagenase appears to be a tetramer with a molecular weight of about 105 000 composed of two different subunits (mol wt 24 000 and 28 000). Some of the properties of the Vibrio collagenase are compared with those of Clostridium histolyticum collagenase. Molecular weights, subunit structures, specificity and mode of collagen hydrolysis, insensitivity to diisopropyl fluorophosphate and calf serum, and sensitivity to certain metal ion complexing agents and isopropyl alcohol are similar for the collagenases from both organisms. However, Vibrio B-30 collagenase and Clostridium collagenase differ immunologically and electrophoretically.

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Section: Methodsmentioning

confidence: 99%

Purification and characterization of a marine bacterial collagenase

Merkel¹,

Dreisbach²

1978

Biochemistry

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“…Small portions of dog Achilles tendon were freed of fascia and were sonicated first in a mixture of chloroform-methanol (1:3, v/v) and then in 0.85 % NaCl to remove lipids and vascular debris. The collagen was then prepared according to the method of Einbinder and Schubert (1951). Bovine Achilles tendon collagen was obtained commercially from Nutritional Biochemicals, Ohio.…”

Section: Preparation Of Glomerular Basement Membranementioning

confidence: 99%