| ¿µ¹® | striated muscle | ÇÑ±Û | °¡·Î¹«´Ì±Ù |
|---|---|---|---|
| ¼³¸í | Ç¥¸é¿¡ °¡·ÎÁÙ¹«´Ì°¡ º¸ÀÌ´Â ±ÙÀ°. ¶æ´ë·Î ¿òÁ÷ÀÏ ¼ö ÀÖÀ¸¹Ç·Î ¼öÀDZÙÀ̶ó°íµµ ºÒ¸°´Ù. ÀÎüÀÇ °¡·Î¹«´Ì±ÙÀÇ ´ëºÎºÐÀº °ñ°Ý±ÙÀ̸ç, ¾ó±¼ÀÇ ÇǺθ¦ ¿òÁ÷À̴ ǥÁ¤±Ù, Çô³ª Èĵθ¦ ¿òÁ÷ÀÌ´Â ±ÙÀ°µµ °¡·Î¹«´Ì±ÙÀÌ´Ù. ¿¹¸¦ µé¾î ÆÈÀ» ±¸ºÎ¸± ¶§´Â ¸¹Àº ±ÙÀ°ÀÇ º¹ÀâÇÑ ÇùÁ¶°¡ ÇÊ¿äÇÏ¿© ÀüüÀûÀÎ ¿òÁ÷ÀÓÀ» ÅëÁ¦ÇÏ´Â ±â±¸°¡ ÀÖ´Ù. ¶Ç ÀÚ¼¼ÀÇ ±ÕÇüÀ» ÀâÀ» ¶§ µî ¸¹Àº ¿îµ¿À» ¹«ÀǽÄÀû-¹Ý»çÀûÀ¸·Î Á¶ÀýÇÏ´Â ±â±¸µµ ÀÖ´Ù. ½ÉÀå±ÙÀº °¡·Î¹«´Ì±ÙÀÌÁö¸¸ ºÒ¼öÀDZÙÀÇ ¼ºÁúÀ» °¡Á³´Ù. |
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| ¿µ¹® | skeletal muscle | ÇÑ±Û | °ñ°Ý±Ù |
|---|---|---|---|
| ¼³¸í | °ñ°Ý¿¡ ºÙ¾î ±× ¿îµ¿À» °üÀåÇÏ´Â ±ÙÀ°°è. °ñ°Ý±Ù-ÆòȰ±Ù-½ÉÀå±Ù µî ¼¼ °³ ±ÙÁ¶Á÷ÀÇ Çϳª. ±½±â 10~100¥ì, ±æÀÌ 5~12cmÀÇ °¡´Ã°í ±ä ±ÙÀ°¼¶À¯ÀÇ ÁýÇÕüÀ̸ç, °¡·Î¹«´Ì°¡ ÀÖ°í, ¼öÀǿÀ» ÇÑ´Ù. ÇÑ °³ÀÇ °ñ°Ý±ÙÀº ´Ù¼öÀÇ ±Ù¼¶À¯¿Í °áÇÕÁ¶Á÷À¸·Î ±¸¼ºµÇ°í °¢±â ƯÀ¯ÇÑ ÇüŸ¦ Áö´Ñ´Ù. ±ÙÀ°ÀÇ ¾ç³¡Àº °¡´Ã¸ç ±× ºÎºÐÀ» ±ÙÀ°¸Ó¸®¶ó°í ÇÑ´Ù. ±ÙÀ°¸Ó¸®´Â ÈûÁÙ·Î ÀÌÇàÇϸç ÈûÁÙÀº »À¸·¿¡ ºÙ´Âµ¥, ¶§·Î´Â »À¸·À» Œä°í »À¿¡ ºÎÂøµÇ¾î ÀÖ´Ù. ±ÙÀ°ÀÇ Á߾Ӻδ ±½°í µÎ²¨¿ì¸ç À̺κÐÀ» ±Ùº¹À̶ó ÇÑ´Ù. ±ÙÀ°¸Ó¸®´Â ´Ù½Ã µÎ°¥·¡±Ù-¼¼°¥·¡±Ù-³×°¥·¡±ÙÀ¸·Î ³ª´¶´Ù. ±ÙÀ°ÀÇ ¿îµ¿ ÀÚü´Â Ç×»ó ±Ù¼¶À¯ÀÇ ¹æÇâ¿¡ µû¸£´Â ¼öÃà¿îµ¿»ÓÀÌ´Ù. ±×·¯³ª °ñ°Ý±ÙÀÌ »À¿¡ ºÙÀº À§Ä¡¿¡ µû¶ó »À´ë¿¡ ´ëÇÑ ¿©·¯ °¡Áö ¿îµ¿À» ÇÏ°Ô µÈ´Ù. ¿îµ¿ÇÏ´Â ÇüÅ·Π°ñ°Ý±ÙÀ» ºÐ·ùÇÏ¸é Æï±Ù-±ÁÈû±Ù-³»Àü±Ù-¿ÜÀü±Ù-ȸ¿Ü±Ù-ȸ³»±Ù-¿Ã¸²±Ù µîÀÌ ÀÖ´Ù. ±ÁÈ÷°í Æï-³»¿ÜÀü-ȸ³»¿ÜÀÇ ¿îµ¿Àº °üÀýÃàÀ» Áß½ÉÀ¸·Î ÇàÇÑ´Ù. °°Àº °ñ°Ý¿¡ ´ëÇÏ¿© Æß±ÙÀ°°ú ±ÁÈû±ÙÀ°ÀÌ °¢±â ¹Ý´ë¿îµ¿À» ÇÒ °æ¿ì¿¡´Â ¾ç ±ÙÀ°À» ¼·Î ´ëÇ×±ÙÀ̶ó Çϰí, °øµ¿¿îµ¿À» ÇÏ´Â °æ¿ì¿¡´Â °øµ¿±ÙÀ̶ó ÇÑ´Ù. |
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| ¿µ¹® | muscle | ÇÑ±Û | ±ÙÀ° |
|---|---|---|---|
| ¼³¸í | ÀǽÄÀÇ Á¶Àý¿©ºÎ¿¡ µû¶ó ¼öÀDZÙ(ÀǽĿ¡ ÀÇÇØ¼ Á¶ÀýÀÌ °¡´ÉÇÑ ±ÙÀ°: ¿¹¸¦ µé¾î ´Ù¸®, ÆÈ, ¾ó±¼±ÙÀ° µî)°ú ºÒ¼öÀDZÙ(Àǽİú ¹«°üÇÏ°Ô Á¶ÀýÇÏÁö ¾Ê¾Æµµ ¿òÁ÷ÀÌ´Â ±ÙÀ°: ¿¹¸¦ µé¾î ½ÉÀå±Ù, ¼Òȱâ°ü¿¡ ºÐÆ÷ÇÏ´Â ±ÙÀ° µî)À¸·Î ³ª´©¾îÁú ¼ö ÀÖÀ¸¸ç, ¶ÇÇÑ ½ÉÀå±ÙÀÌ µû·Î Á¸ÀçÇÑ´Ù. |
||
| ¿µ¹® | muscle biopsy | ÇÑ±Û | ±ÙÀ°»ý°Ë |
|---|---|---|---|
| ¼³¸í | »ýü³»¿¡¼ ±ÙÀ°¿¡ ´ëÇÑ Áúº´ÀÇ °¨º°Áø´ÜÀ» À§Çؼ ½Ç½ÃÇÏ´Â °Ë»ç¹ý. ¹æ¹ýÀº º´ÅͰ¡ ÀÖ´Â ºÎÀ§³ª ȤÀº ¾ø¾îµµ Å©°Ô Ȱµ¿¿¡ ÁöÀåÀÌ ¾ø´Â ±ÙÀ°ºÎÀ§ÀÇ Á¶Á÷À» ¶¼¾î Çö¹Ì°æÀûÀ¸·Î °Ë»çÇÑ´Ù. ¿¹¸¦ µé¾î ½Å°æÁ¶Á÷ÀÇ ÀÌ»óÀ¸·Î ÀÎÇÑ ±ÙÀ°º´ÅÍÀÇ °æ¿ì, ±ÙÀ°»ý°ËÀ» ÇÏ¿© °üÂûÇØº¸¸é À̸¥¹Ù ¡°¹«¸®Áø À§Ãà(grouped atrophy)¡±ÀÌ ³ªÅ¸³ª¼, ´Ù¸¥ º´ÅÍ¿¡ ÀÇÇÑ °Í°ú °¨º°ÀÌ °¡´ÉÇÏ´Ù. |
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| MR | Maddox rods; magnetic resistance; magnetic resonance; mandibular reflex; mannose-resistant; may repe... |
|---|---|
| ASM | acid sphingomyelinase; airway smooth muscle; American Society for Microbiology; anterior scalenus mu... |
| CM | California mastitis [test]; calmodulin; capreomycin; carboxymethyl; cardiac murmur; cardiac muscle; ... |
| LM | lactic acid mineral [medium]; lactose malabsorption; laryngeal mask; laryngeal muscle; lateral malle... |
| MG | Marcus Gunn [pupil]; margin; medial gastrocnemius [muscle]; membranous glomerulonephritis; menopausa... |
| GP | Glycogen Phosphorylase |
|---|---|
| MTAP | Methylthioadenosine phosphorylase |
| NP | Nucleoside phosphorylase |
| PHK | Phosphorylase kinase |
| PD-ECGF/TP | Platelet-derived endothelial cell growth factor/thymidine phosphorylase |
| muscle phosphorylase deficiency | Type V glycogen storage disease, affecting muscle, caused by deficiency of muscle phosphorylase. (05 Mar 2000) |
|---|
| alpha,alpha-trehalose phosphorylase | <enzyme> Chemical name: alpha-d-glucopyranosyl-alpha-d-glucopyranose orthophosphate glucosyltransferase Registry number: EC 2.4.1.64 Synonym: trehalose phosphorylase (26 Jun 1999) |
|---|---|
| alpha-glucan phosphorylase | <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase). (21 Jun 2000) |
| maltodextrin phosphorylase | <enzyme> From E coli Registry number: EC 2.4.1.- Synonym: e350a (26 Jun 1999) |
| GDPmannose phosphorylase | <enzyme> A transferase that catalyses the transfer of GDP to the mannose of mannose-1-phosphate. Consider also the bifunctional enzyme, phosphomannose isomerase-guanosine diphospho-d-mannose pyrophosphorylase; rfbm has similarity to long-chain, iron-containing alcohol dehydrogenases Registry number: EC 2.7.7.13 Synonym: GDPmannose phosphorylase, GDP mannose pyrophosphorylase, GTP-alpha-d-mannose-1-phosphate guanylyltransferase, GDP-mannose pyrophosphorylase, rfbm gene product, rfbm protein (26 Jun 1999) |
| cellodextrin phosphorylase | <enzyme> Reverse reaction is used to synthesise cellodextrins Registry number: EC 2.4.1.49 (26 Jun 1999) |
| glycogen phosphorylase | <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase). (21 Jun 2000) |
| phosphorylase | <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase). (21 Jun 2000) |
| phosphorylase a | <enzyme> The phosphorylated and more active form of phosphorylase that functions as a regulatory enzyme during glycogen breakdown. The phosphate groups are hydrolytically removed by phosphorylase phosphatase to form phosphorylase b and orthophosphate. Registry number: EC 2.4.1.- (12 Dec 1998) |
| phosphorylase b | <enzyme> The relatively inactive form of phosphorylase that is reactivated to form phosphorylase a by phosphorylase kinase, which catalyses the enzymatic phosphorylation of the serine residues at the expense of ATP. Registry number: EC 2.4.1.- (12 Dec 1998) |
| phosphorylase kinase | <enzyme> The enzyme that regulates the activity of phosphorylase and glycogen synthetase by addition of phosphate groups. A large and complex enzyme, itself regulated by phosphorylation. Integrates the hormonal and calcium signals in muscle. (18 Nov 1997) |
| phosphorylase kinase phosphatase | <enzyme> Aspect of phosphoprotein phosphatase EC 3.1.3.16 Registry number: EC 3.1.3.- (26 Jun 1999) |
| phosphorylase phosphatase | <enzyme> An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form. Chemical name: (Phosphorylase a) phosphohydrolase Registry number: EC 3.1.3.17 (12 Dec 1998) |
| phosphorylase-rupturing enzyme | <enzyme> An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form. Chemical name: (Phosphorylase a) phosphohydrolase Registry number: EC 3.1.3.17 (12 Dec 1998) |
| polynucleotide phosphorylase | <enzyme> An enzyme of the transferase class that catalyses the reaction RNA(n+1) and orthophosphate to yield RNA(n) and a nucleoside diphosphate, or the reverse reaction. ADP, idp, GDP, udp, and cdp can act as donors in the latter case. Chemical name: Polyribonucleotide:orthophosphate nucleotidyltransferase Registry number: EC 2.7.7.8 (12 Dec 1998) |
| xanthosine phosphorylase | <enzyme> From E coli k-12; mw 18kda; inactivated by p-chloromercuriphenylsulfonic acid Registry number: EC 2.4.2.- Synonym: inosine-guanosine phosphorylase (26 Jun 1999) |
| muscle phosphorylase |
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|---|---|
| muscle phosphorylase deficiency |
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