Studies on the composition of the extracellular fluid from calf costal cartilage

Rabadjija, Luka; Koren, Eugen; Pende, B

doi:10.1016/0304-4165(71)90196-6

Cited by 9 publications

(3 citation statements)

References 18 publications

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“…Fig. 2 (Strauch & Vencelj, 1967), a variety of tissues taken from rabbits (Espey & Rondell, 1967), fibrotic liver (Sakai et al, 1967), mouse fibroblast cells, liver, bone and skin of the chick embryo (Strauch, Vencelj & Hannig, 1968), tadpole tail fin (Harper & Gross, 1970), calf costal cartilage (Rabadjija, Koren & Pende, 1971) and in Graafian follicles (Espey & Rondell, 1965). Although these enzymes cannot be considered true collagenases because they do not degrade native collagen, they do possess specificity for -Pro-x-Gly-Pro-y sequence according to some authors (Strauch, 1970;Woessner, 1970) and probably participate in the final stages of collagen degradation (Harper & Gross, 1970).…”

Section: Resultsmentioning

confidence: 99%

`Collagenase-Like' Peptidase in Human, Rat and Bull Spermatozoa

Koren¹,

Milković²

1973

Reproduction

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Summary. A peptidase capable of splitting synthetic collagenase substrate and collagen peptides,`collagenase-like' peptidase, has been discovered in human semen, rat and bull epididymal spermatozoa and rat and bull testes. This enzyme is also present in human seminal plasma and sperm washings, but its total activity pattern in human semen fractions, its specific activity in washed spermatozoa and the negligible activity found in the azo\l=o"\spermicejaculate prove that it is a sperm enzyme. As shown by the thin-layer chromatography of the reaction products,`collagenase-like' peptidase cleaves synthetic collagenase substrate at the same site as bacterial collagenase does. The pH optimum of the`c ollagenase-like' peptidase is 7\m=.\5.The enzyme has been partially purified from rat testis homogenate by ammonium sulphate saturation and gel filtration on a Sephadex G-200 column. Its molecular weight appears to be about 110,000. The possible r\l=o^\leof this enzyme in fertilization is discussed.

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Section: Resultsmentioning

confidence: 99%

`Collagenase-Like' Peptidase in Human, Rat and Bull Spermatozoa

Koren¹,

Milković²

1973

Reproduction

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“…Enzymes that can degrade synthetic collagenase substrate have been detected in a number of different animal tissues (Sakai et al 1967; Strauch & Vencelj, 1967;Cutroneo & Fuller, 1970;Rabadjija, Koren & Pende, 1971 ; Levdikova & Orekovich, 1972;Aswanikumar & Radhakrishnan, 1972 and are believed to play some role in the degradation of extracellular proteins, although their properties have not been studied in detail. Woessner (1970) reported that such an enzyme, obtained from chick embryos, required Ca++ for its activity, but no metal requirement was found for the enzyme from rat granuloma tissue (Aswanikumar & Radhakrishnan, 1972).…”

Section: Introductionmentioning

confidence: 99%

The metalloenzymic nature of collagenase-like peptidase of the rat testis

Lukač¹,

Koren²

1977

Reproduction

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Summary. Collagenase-like peptidase, an enzyme degrading synthetic collagenase substrate (PZ-pentapeptide), was purified from rat testes and its properties were examined. Its activity was strongly inhibited by chelating agents, such as EDTA and 1,10-phenanthroline. By chelation and exhaustive dialysis it was possible to obtain this enzyme in its inactive, metal-free form. The activity of the metal-free enzyme was partly recovered by treatment with zinc or manganese ions, while a combined zinc and manganese treatment resulted in complete recovery of enzyme activity.

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“…In tissues there seems to be a relatively heatstable collagen-labilizing or collagenolytic factor ( c f . Rabadjija et al 1971). Kuhn et al (1964) observed that purified tropocollagen does not aggregate so well as less purified samples.…”

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confidence: 99%

Assay of the Transformation of Collagen in situ

Heikkinen¹,

Ivaska²,

Kulonen³

1972

Acta Physiologica Scandinavica

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HEIRKISEN E.. K. I V A S K -~ and E. KVLOSES. Atsay of the fmnsformatioti of collagcii in situ. . k t a physiol. scand. 1972. 84. 550-554.Skin extract of newborn rats increases the insolubilization of collagen in skin slices in citro. The effect is destroyed by heating and inhibited by lathyrogens. Purified collagen in the precipitated forni ia. on the contrary. transformed to the more soluble forms by skin extract.

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Studies on the composition of the extracellular fluid from calf costal cartilage

Cited by 9 publications

References 18 publications

`Collagenase-Like' Peptidase in Human, Rat and Bull Spermatozoa

`Collagenase-Like' Peptidase in Human, Rat and Bull Spermatozoa

The metalloenzymic nature of collagenase-like peptidase of the rat testis

Assay of the Transformation of Collagen in situ

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