1991NIPPON SUISAN GAKKAISHIOpen access

Hydrolytic Action of Salmon Cathepsins B and L to Muscle Structural Proteins in Respect of Muscle Softening.

Michiaki Yamashita, Shiro Konagaya

Open full text 125 citations

Abstract

Cathepsins B and L, lysosomal cysteine proteases, are suspected of causing the softening phenomenon of post-mortem muscle of salmon. The proteolytic action of these enzymes on structural proteins of fish muscle was investigated. Cathepsin L was capable of hydrolyzing the major muscle structural proteins, such as connectin, nebulin, myosin, collagen, α-actinin, and troponins T and I. Although cathepsin B hydrolyzed connectin, nebulin, and myosin, the hydrolysis rate was very low and, furthermore, the hydrolytic action was limited to only these proteins. These findings indicate the direct participation of cathepsin L in drastic proteolytic degradation of the fine structure of muscle of the fish.

Open-access reader

About this research paper

What this paper is about

Cathepsins B and L, lysosomal cysteine proteases, are suspected of causing the softening phenomenon of post-mortem muscle of salmon. The proteolytic action of these enzymes on structural proteins of fish muscle was investigated. Cathepsin L was capable of hydrolyzing the major muscle structural proteins, such as connectin, nebulin, myosin, collagen, α-actinin, and troponins T and I. Although cathepsin B hydrolyzed connectin, nebulin, and myosin, the hydrolysis rate was very low and, furthermore, the hydrolytic action was limited to only these proteins. These findings indicate the direct participation of cathepsin L in drastic proteolytic degradation of the fine structure of muscle of the fish.

Why it matters

OpenAlex reports 125 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Cathepsins B and L, lysosomal cysteine proteases, are suspected of causing the softening phenomenon of post-mortem muscle of salmon. The proteolytic action of these enzymes on structural proteins of fish muscle was investigated. Cathepsin L was capable of hydrolyzing the major muscle structural proteins, such as connectin, nebulin, myosin, collagen, α-actinin, and troponins T and I. Although cathepsin B hydrolyzed connectin, nebulin, and myosin, the hydrolysis rate was very low and, furthermore, the hydrolytic action was limited to only these proteins. These findings indicate the direct participation of cathepsin L in drastic proteolytic degradation of the fine structure of muscle of the fish.

Key concepts: Nebulin, Myosin, Cathepsin, Biochemistry, Cathepsin B, Chemistry, Cathepsin L, Proteolysis

Related papers

Back to paper searchBrowse research topicsOriginal source
Hydrolytic Action of Salmon Cathepsins B and L to Muscle Structural Proteins in Respect of Muscle Softening. — Research Paper | ScholarLens