Recombinant Human Hyaluronidase (PH20) belongs to a family of enzymes that catalyze the degradation of hyaluronic acid and can degrade hyaluronic acid in the extracellular matrix and promote the diffusion of extracellular substances.
Hyaluronidase (HAse) is a type of glycosylase widely distributed in nature and degrades hyaluronic acid (HA) by acting on β-1, 3 or β-1,4-glycosidic bonds. In addition, it also catalyzes the action of chondroitin (CS) and chondroitin sulfate to some extent. Hyaluronidase was first discovered in 1929. Scientists discovered a "diffusion factor" that promotes the spread of vaccines, dyes, and toxins in the mammalian testis and other extracts. It was subsequently identified as hyaluronidase.
Hyaluronidase is widely found in body fluids such as animal plasma, tissue fluids, and semen, organs such as kidney, liver, spleen, and brain, animal venoms such as snake venom, lizard poison, scorpion venom, spider venom, bee venom, and ant poison, as well as some bacteria.
Hyaluronidase is present in many animal venoms. The activity of hyaluronidase has been detected in the venom of bees, snakes, spiders, rose locusts, lizards and scorpions. Hyaluronidase degrades the hyaluronic acid in the perivascular matrix to make the toxin easily accessible to blood vessels, which is the key to the entry of venom into the systemic circulation from the site of injury. From the isoelectric point, hyaluronidase in animal venom is a basic protein, approximately 33-110 kDa. The hyaluronidases in bee venom are allergens that cause the body to produce IgE-mediated, fatal allergic reactions. Structural analysis of hyaluronidase in venom has important clinical significance and provides a basis for the pathological response to the venom.
Hyaluronidase is a virulence factor in the pathogenic process of microorganisms. It is usually in direct contact with host tissues or causes pathogens to escape their defense mechanisms. Hyaluronidase degrades hyaluronic acid in the host matrix, making the host susceptible to gas gangrene, meningitis, synovitis, hyperplasia, nephritis, mycoplasmosis, periodontal disease, mastitis, pneumonia, sepsis, syphilis, toxic shock syndrome and other diseases. The high-molecular-weight hyaluronic acid in the host body is involved in immune regulation and has anti-inflammatory activity, and the hyaluronidase produced by the microorganism cleaves the high-molecular-weight hyaluronic acid contained therein into oligomeric hyaluronic acid and becomes a factor for inducing an inflammatory reaction, molding the environment for the growth of microorganisms in the host organism.
Recombinant Human Hyaluronidase (PH20) belongs to a family of enzymes that catalyze the degradation of hyaluronic acid and can degrade hyaluronic acid in the extracellular matrix and promote the diffusion of extracellular substances.
Hyaluronidase (HAse) is a type of glycosylase widely distributed in nature and degrades hyaluronic acid (HA) by acting on β-1, 3 or β-1,4-glycosidic bonds. In addition, it also catalyzes the action of chondroitin (CS) and chondroitin sulfate to some extent. Hyaluronidase was first discovered in 1929. Scientists discovered a "diffusion factor" that promotes the spread of vaccines, dyes, and toxins in the mammalian testis and other extracts. It was subsequently identified as hyaluronidase.
Hyaluronidase is widely found in body fluids such as animal plasma, tissue fluids, and semen, organs such as kidney, liver, spleen, and brain, animal venoms such as snake venom, lizard poison, scorpion venom, spider venom, bee venom, and ant poison, as well as some bacteria.
Hyaluronidase is present in many animal venoms. The activity of hyaluronidase has been detected in the venom of bees, snakes, spiders, rose locusts, lizards and scorpions. Hyaluronidase degrades the hyaluronic acid in the perivascular matrix to make the toxin easily accessible to blood vessels, which is the key to the entry of venom into the systemic circulation from the site of injury. From the isoelectric point, hyaluronidase in animal venom is a basic protein, approximately 33-110 kDa. The hyaluronidases in bee venom are allergens that cause the body to produce IgE-mediated, fatal allergic reactions. Structural analysis of hyaluronidase in venom has important clinical significance and provides a basis for the pathological response to the venom.
Hyaluronidase is a virulence factor in the pathogenic process of microorganisms. It is usually in direct contact with host tissues or causes pathogens to escape their defense mechanisms. Hyaluronidase degrades hyaluronic acid in the host matrix, making the host susceptible to gas gangrene, meningitis, synovitis, hyperplasia, nephritis, mycoplasmosis, periodontal disease, mastitis, pneumonia, sepsis, syphilis, toxic shock syndrome and other diseases. The high-molecular-weight hyaluronic acid in the host body is involved in immune regulation and has anti-inflammatory activity, and the hyaluronidase produced by the microorganism cleaves the high-molecular-weight hyaluronic acid contained therein into oligomeric hyaluronic acid and becomes a factor for inducing an inflammatory reaction, molding the environment for the growth of microorganisms in the host organism.
