Bull Semen Ribonucleases. 1. Purification and Physico-Chemical Properties of the Major Component

D’Alessio, Giuseppe; Flobidi, Ardesio; Prisco, Rocco De; A, Pignero; Leone, E

doi:10.1111/j.1432-1033.1972.tb01751.x

Cited by 116 publications

(49 citation statements)

References 40 publications

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“…RNase BS is a basic protein with an isoelectric point G-actin (12 pM) was incubated with an equal volume of 3.6 pM RNase BS. Samples were taken at different times and assayed for enzymatic activity around 10.5 [3]. For the more acidic actin this value is around 5.4 [18].…”

Section: Discussionmentioning

confidence: 99%

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On the interaction of bovine seminal RNase with actin in vitro

Simm¹,

Krietsch²,

Isenberg³

1987

Eur J Biochem

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Ribonuclease from bovine seminal plasma (RNase BS) interacts with skeletal muscle actin in the following way: it (1) binds to actin with an apparent binding constant of 9.2 x lo4 M-' in 0.1 M KC1, (2) induces the polymerization of actin below the critical concentration in depolymerization buffer, (3) accelerates the salt-induced polymerization of actin even at a molar ratio of RNase to actin lower than l / l O O , and (4) bundles F-actin filaments. In the bundles the molar ratio of RNase to actin is about 0.66. (5) Actin inhibits the enzymatic activity of RNase BS.RNase A from bovine pancreas, which is structurally almost identical to the subunits of RNase BS as well as a monomeric form of RNase BS, do not cross-link actin filaments and have a much smaller effect on the polymerization of actin.We conclude that the dimeric structure of the RNase BS, which consists of two identical subunits cross-linked by interchain disulfide bridges, is probably responsible for the bundling activity and the accelerating effect on the polymerization of actin.Many proteins have been discovered which interact with actin, the major component of the eucaryotic cytoskeleton [l]. Most of these proteins were isolated with the aim of investigating their regulating effect on actin polymerization in vitro and the possible interconversion of different actin structures inside the cell.Among those the protein pancreatic DNase I gained special attention, since it was found that DNase I depolymerizes F-actin to form a 1 : l complex with G-actin [2], although its physiological relevance remains questionable. In this context it was of interest to look for a possible interaction of the complementary protein pancreatic RNase A with actin. We show here that only the dimeric RNase [3,4], a cytotoxic substance [5,6] from bovine seminal plasma, strongly interacts with actin as a gelation, bundling, and nucleation factor. MATERIALS AND METHODS Preparation of proteinsAll preparations were carried out at 4°C. Rabbit skeletal muscle actin was prepared according to Spudich and Watt [7].

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Section: Discussionmentioning

confidence: 99%

“…In this context it was of interest to look for a possible interaction of the complementary protein pancreatic RNase A with actin. We show here that only the dimeric RNase [3,4], a cytotoxic substance [5,6] from bovine seminal plasma, strongly interacts with actin as a gelation, bundling, and nucleation factor. …”

mentioning

confidence: 99%

On the interaction of bovine seminal RNase with actin in vitro

Simm¹,

Krietsch²,

Isenberg³

1987

Eur J Biochem

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“…It can be isolated from bull seminal plasma [4] or from bull seminal vesicles [5,6], the organ where it is produced. The primary structure of the subunit chain [ 1,7-91 is strictly homologous to that of pancreatic RNase A from the same species.…”

Section: Introduction 2 Materials and Methodsmentioning

confidence: 99%

“…Non-hyperbolic saturation curves have been occasionally reported [ 13 ,141 for a small number of oligomeric enzymes, but to our knowledge never for a dimeric enzyme. BS-RNase was prepared from bull seminal plasma [4] and bull seminal vesicles [6] as described. The enzyme preparations used in these experiments were homogeneous by polyacrylamide gel electrophoresis in the presence [I] and absence [4] of SDS and by amino acid analysis [4].…”

Section: Introduction 2 Materials and Methodsmentioning

confidence: 99%

Bovine seminal ribonuclease: Non‐hyperbolic kinetics in the second reaction step

et al. 1982

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“…Recently, however, it has been shown [ 71 that double-stranded RNA and the poly(A)* poly(U) complex are degraded by RNAase BS-1, a ribonuclease isolated from bovine seminal plasma [8,9] , which has been found to be composed of two identical subunits, each containing the structural elements of RNAase A active site [ 10, 111.…”

Section: Introductionmentioning

confidence: 99%