¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"trypsin thrombin"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
¿µ¹® thrombin ÇÑ±Û Æ®·Òºó
¼³¸í   
  ÇÁ·ÎÆ®·Òºó¿¡¼­ À¯·¡µÇ´Â È¿¼Ò·Î¼­, ¼¶À¯¼Ò¿øÀ» ¼¶À¯¼ÒÀ¸·Î º¯È¯½ÃÄÑ Ç÷¾×ÀÀ°í¸¦ ¿Ï¼º½ÃŲ´Ù.
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 3 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • trypsin
    Æ®¸³½Å
  • thrombin
    Æ®·Òºó
  • thrombin time
    Æ®·Òºó½Ã°£
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 3 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • trypsin
    Æ®¸³½Å
  • thrombin
    Æ®·Òºó
  • thrombin time
    Æ®·Òºó½Ã°£
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • inter-alpha-trypsin inhibitor
    ÀÎÅÍ-¾ËÆÄ-Æ®¸³½Å ¾ïÁ¦Á¦
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • trypsin thrombin
    Æ®¸³½ÅÆ®·Òºó.
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • inter-alpha-trypsin inhibitor
    ÀÎÅÍ-¾ËÆÄ-Æ®¸³½Å ¾ïÁ¦Á¦
  • trypsin
    Æ®¸³½Å.
  • trypsin
    Æ®¸³½Å
  • trypsin inhibitor
    Æ®¸³½Å¾ïÁ¦Á¦(¡­åäð¤ð¥).
  • trypsin inhibitor
    Æ®¸³½Å¾ïÁ¦Á¦(¡­åäð¤ð¥)
  • trypsin test
    Æ®¸³½Å½ÃÇè(¡­ãËúÐ)
  • trypsin-like immunoreactivity(TLI)
  • serial thrombin time
    ¿¬¼ÓÆ®·Òºó½Ã°£(ææáÙ¡­ ãÁÊà).
  • serial thrombin time
    ¿¬¼ÓÆ®·Òºó½Ã°£(ææáÙ¡­ ãÁÊà)
  • thrombin
    Æ®·Òºó
  • thrombin
    Æ®·Òºó.
  • thrombin
    Æ®·Òºó
  • thrombin coinhibitor
    Æ®·ÒºóÄÚÀÎÈ÷ºñÅÍ, Æ®·Òºóº¸Á¶¾ïÁ¦ÀÎÀÚ.
  • thrombin time
  • thrombin time=TT
    Æ®·Òºó½Ã°£
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 4 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • citrate-activated thrombin
    ½ÃÆ®¸£»êȰ¼º(ß«üÀàõ) Æ®·Òºó
  • soybean trypsin inhibitor
    ´ëµÎ(ÓÞÔç) Æ®¸³½Å ÀúÇØÁ¦(îÁúªð¥)
  • thrombin
    Æ®·Òºó
  • trypsin
    Æ®¸³½Å
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • thrombin
    Æ®·Òºó
  • trypsin
    Æ®¸³½Å
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
BPTI basic pancreatic trypsin inhibitor; basic polyvalent trypsin inhibitor; bovine pancreatic trypsin in...
PTI pancreatic trypsin inhibitor; persistent tolerant infection; Pictorial Test of Intelligence; placent...
STI Scientific and Technical Information; serum trypsin inhibitor; soybean trypsin inhibitor; systolic t...
TT   1) Thrombin Time
  2) Transient Thyrotoxicosis
HT Hashimoto thyroiditis; hearing test; hearing threshold; heart; heart transplantation, heart transpla...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
AT III Anti-thrombin III
BPTI Basic Pancreatic Trypsin Inhibitor
BPTI Bovine Pancreatic Trypsin Inhibitor
IRT Immunoreactive trypsin
ITI Inter-Alpha-Trypsin Inhibitor
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • thrombin
    ±â°£ ¼¼Æ÷, Æ®·Òºó
    1. ÀÀÇ÷ ÀÛ¿ëÀ» ÇÏ´Â ÇͼÓÀÇ È¿¼Ò. 2. ÇÁ·ÎÆ®·Òºó¿¡¼­ À¯·¡µÇ´Â È¿¼Ò·Î¼­, ÇǺ긮³ëÁ¨À» ÇǺ기À¸·Î º¯È¯ÇÑ´Ù. 3. Ä®½·ÀÇ Á¸Àç ÇÏ¿¡¼­ ÷°¡µÈ Æ®·Òº¸ÇÃ¶ó½ºÆ¾°úÀÇ »óÈ£ÀÛ¿ë¿¡ ÀÇÇØ¼­ ¼Ò¿¡¼­ À¯·¡µÈ ÇÁ·ÎÆ®·ÒºóÀ¸·ÎºÎÅÍ ¸¸µé¾îÁø ¹«±Õ ´Ü¹é¹°ÁúÀÇ Á¦Á¦·Î¼­ ±¹¼Ò ÁöÇ÷Á¦·Î »ç¿ëµÈ´Ù. 4. ÇöÀå ¼ÓÀÇ ÇÁ·ÎÆ®·ÒºóÀÌ È°¼ºÈ­µÈ ÀÀÇ÷ ¿ä¼Ò·Î ¼¶À¯¼Ò¿øÀ» ¼¶À¯¼Ò·Î ÀüÈ­ÇÏ´Â È¿¼Ò coagulaseÀÇ Çϳª. 5. ÀÀ°í¿¡ À־ fibrinogenÀ» fibrinÀ¸·Î º¯È­½ÃŰ´Â È¿¼Ò.
  • trypsin
    Æ®¸³½Å
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
receptors, thrombin Cell surface proteins that specifically bind thrombin and trigger changes in the behaviour of blood cells. There are at least two types of thrombin receptors on platelets. The higher affinity receptors mediate the inhibition of stimulated adenylate cyclase, the secretion of acid hydrolases, and the activation of phospholipase a2. The lower affinity receptors are linked to phospholipase c and trigger platelet aggregation and exposure of fibrinogen binding sites. A human platelet thrombin receptor has been cloned and is a member of the family of peptide receptors. There are also thrombin receptors on endothelial cells and smooth muscle cells.
(12 Dec 1998)
human thrombin Thrombin obtained from human plasma by precipitation with suitable salts and organic solvents; same uses as thrombin.
(05 Mar 2000)
thrombin <enzyme> Protease (34 kD) generated in blood clotting that acts on fibrinogen to produce fibrin. Consists of two chains, A and B, linked by a disulphide bond. B chain has sequence homology with pancreatic serine proteases: cleaves at Arg Gly.
Thrombin is produced from prothrombin by the action either of the extrinsic system (tissue factor + phospholipid) or, more importantly, the intrinsic system (contact of blood with a foreign surface or connective tissue). Both extrinsic and intrinsic systems activate plasma factor X to form factor Xa which then, in conjunction with phospholipid (tissue derived or platelet factor 3) and factor V, catalyses the conversion.
(18 Nov 1997)
thrombin time Test of the conversion of fibrinogen to fibrin by thrombin in which clotting time of plasma mixed with a thrombin solution is measured. Time is prolonged by afibrinogenaemia, abnormal fibrinogen, or the presence of inhibitory substances, e.g., fibrin-fibrinogen degradation products, heparin. Reptilase, a thrombin-like enzyme unaffected by the presence of heparin, may be used in place of thrombin.
(12 Dec 1998)
a1-trypsin inhibitor A glycoprotein that is the major protease inhibitor of human serum, is synthesised in the liver, and is genetically polymorphic due to the presence of over 20 alleles; individuals appropriately homozygous are deficient in a1-trypsin and are predisposed to pulmonary emphysema and juvenile hepatic cirrhosis because of alterations in the amino acid and sialic acid components of the glycoprotein. A1-Antitrypsin also inhibits thrombin.
Synonym: a1-trypsin inhibitor, human a1-proteinase inhibitor.
(05 Mar 2000)
Artemia trypsin-like proteinase <enzyme> Cysteine proteinase involved in lipovitellin degradation
Registry number: EC 3.4.22.-
(26 Jun 1999)
crystallised trypsin A purified preparation of the pancreatic enzyme; used as an adjunct to surgery for debridement of necrotic wounds and ulcers.
(05 Mar 2000)
soybean trypsin inhibitor Single polypeptide (21 kD, 181 amino acids) that forms a stable, stoichiometric, enzymically inactive complex with trypsin.
(18 Nov 1997)
trypsin <enzyme> Serine protease from the pancreas of vertebrates. Cleaves peptide bonds involving the amino groups of lysine or arginine.
(18 Nov 1997)
trypsin G-banding stain <technique> A unique chromosome staining technique, used in human cytogenetics to identify individual chromosomes, which produces characteristic bands.
It utilises acetic acid fixation, air drying, denaturing chromosomes mildly with proteolytic enzymes, salts, heat, detergents, or urea, and finally Giemsa stain; chromosome bands appear similar to those fluorochromed by Q-banding stain.
Synonym: Giemsa chromosome banding stain.
(05 Mar 2000)
trypsin inhibitor A peptide hydrolyzed off trypsinogen under the catalytic influence of enteropeptidase, with trypsin produced as a result; so called because the peptide masks or inhibits the active site of the trypsin molecule, one of the polypeptides, from various sources (e.g., human and bovine colostrum, soybeans, egg white), that inhibit the action of trypsin.
Compare: Bowman-Birk inhibitor.
(05 Mar 2000)
trypsin inhibitor, bowman-birk soybean <chemical> A low-molecular-weight protein (minimum molecular weight 8000) which has the ability to inhibit trypsin as well as chymotrypsin at independent binding sites. It is characterised by a high cystine content and the absence of glycine.
Pharmacological action: trypsin inhibitors.
(12 Dec 1998)
trypsin inhibitor, kazal pancreatic <chemical> A pancreatic trypsin inhibitor common to all mammals. It is secreted with the zymogens into the pancreatic juice. It is a protein composed of 56 amino acid residues and is different in amino acid composition and physiological activity from the kunitz bovine pancreatic trypsin inhibitor (aprotinin).
Chemical name: Trypsin inhibitor, pancreatic secretory
(12 Dec 1998)
trypsin inhibitor, kunitz soybean <chemical> A high-molecular-weight protein (approximately 22,500) containing 198 amino acid residues. It is a strong inhibitor of trypsin and human plasmin.
Pharmacological action: trypsin inhibitors.
Chemical name: Trypsin inhibitor, Kunitz soybean
(12 Dec 1998)
trypsin inhibitors Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.
(12 Dec 1998)
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • thrombin
    Æ®·Òºó(Ç÷¾×ÀÇ ÀÀÇ÷ÀÛ¿ëÀ» ÇÏ´Â È¿¼Ò)
  • trypsin
    Æ®¸³½Å(Ãé¾× ÁßÀÇ ¼ÒÈ­ È¿¼Ò)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 1
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü À¯»ç °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ ¸ÂÃã °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 1
Á¦Ç°¸í
ÆÇ¸Å»ç
º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
±¸ºÐ/º¸Çè±Þ¿©
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ À¯»ç °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 1
Á¦Ç°¸í
ÆÇ¸Å»ç
º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
±¸ºÐ/º¸Çè±Þ¿©
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference ¸ÂÃã °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference À¯»ç °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition ¸ÂÃã °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition À¯»ç °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 1
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
KMLE À¥ ¿ë¾î À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
ÇÑ¿µ/¿µÇÑ »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 1
ÅëÇÕ°Ë»ö ¿Ï·á